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Journal articles on the topic 'Kuruma prawns'

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Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Chen, Ferng-Ruey, Ping-Chung Liu, and Kuo-Kau Lee. "Lethal Attribute of Serine Protease Secreted by Vibrio alginolyticus Strains in Kuruma Prawn Penaeus japonicus." Zeitschrift für Naturforschung C 55, no. 1-2 (February 1, 2000): 94–99. http://dx.doi.org/10.1515/znc-2000-1-218.

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Abstract Toxicity of the extracellular products (ECP) and the lethal attribute of serine protease secreted by five pathogenic Vibrio alginolyticus strains from various sources in kuruma prawn Penaeus japonicus were studied. The ECPs of organisms originally isolated from diseased kuruma prawn or small abalone Haliotis diversicolor supertexta were more lethal (LD50 value of 0.48 or 0.41 μg protein/g prawn) than those from diseased tiger prawn P.monodon, yellowfin porgy Acanthopagrus latus or horse mackerel (LD50 value of 0.98 -1.17 μg protein/g prawn). All the ECPs manifested strong, weak and no activities against gelatin, sheep erythrocytes and chitin, respectively. In immunodiffusion tests using rabbit antiserum to a purified 33 kDa serine protease of strain Swy against ECP of each tested strain produced one single precipitation band in each treatment. Furtherm ore, the serine protease was suggested to be the dominant protease secreted by V. alginolyticus strains tested since the majority of enzymatic activity of the respective ECP was inhibited by phenylmethanesulfonyl fluoride (PMSF). A higher inhibition of serine protease activity by PMSF resulted in lower mortality rate of the ECPs injected into the prawns suggesting that the protease is one of the major lethal factor(s) secreted by Valginolyticus.

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2

ISHIMARU, K., M. AKAGAWA-MATSUSHITA, and K. MUROGA. "Vibrio penaeicida sp. nov., a Pathogen of Kuruma Prawns (Penaeus japonicus)." International Journal of Systematic Bacteriology 45, no. 1 (January 1, 1995): 134–38. http://dx.doi.org/10.1099/00207713-45-1-134.

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3

TAKAHASHI, Yukinori, Toshiaki ITAMI, Atsushi NAKAGAWA, Hiroyuki NISHIMURA, and Toshio ABE. "Studies on the Vibriosis of cultured kuruma prawns Penaeus japonicus BATE - II. Therapeutic effects of oxytetracycline trial tablets against vibriosis in cultured kuruma prawns Penaeus japonicus BATE." NIPPON SUISAN GAKKAISHI 51, no. 10 (1985): 1639–43. http://dx.doi.org/10.2331/suisan.51.1639.

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4

Liu, Ping-Chung, Kuo-Kau Lee, Kah-Ching Yii, Guang-Hsiung Kou, and Shiu-Nan Chen. "News & Notes: Isolation of Vibrio harveyi from Diseased Kuruma Prawns Penaeus japonicus." Current Microbiology 33, no. 2 (August 1, 1996): 129–32. http://dx.doi.org/10.1007/s002849900087.

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5

Okumura, Takuji. "Effects of Bilateral and Unilateral Eyestalk Ablation on Vitellogenin Synthesis in Immature Female Kuruma Prawns, Marsupenaeus japonicus." Zoological Science 24, no. 3 (March 2007): 233–40. http://dx.doi.org/10.2108/zsj.24.233.

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6

YAMAGUCHI, Tadanori, Shiro ITO, Katsuyuki HAMASAKI, and Shuichi KITADA. "Stocking effectiveness of hatchery-released kuruma prawns estimated by two-stage sampling of commercial catch in Ariake Sound, Japan." Fisheries Science 72, no. 2 (April 2006): 233–38. http://dx.doi.org/10.1111/j.1444-2906.2006.01143.x.

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7

Koshio, Shunsuke, Shin-ichi Teshima, Akio Kanazawa, and Takahiro Watase. "The effect of dietary protein content on growth, digestion efficiency and nitrogen excretion of juvenile kuruma prawns, Penaeus japonicus." Aquaculture 113, no. 1-2 (June 1993): 101–14. http://dx.doi.org/10.1016/0044-8486(93)90344-x.

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8

Wang, Yingjie, Jiachen Zang, Chengtao Wang, Xiuqing Zhang, and Guanghua Zhao. "Structural Insights for the Stronger Ability of Shrimp Ferritin to Coordinate with Heavy Metal Ions as Compared to Human H-Chain Ferritin." International Journal of Molecular Sciences 22, no. 15 (July 23, 2021): 7859. http://dx.doi.org/10.3390/ijms22157859.

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Although apoferritin has been widely utilized as a new class of natural protein nanovehicles for encapsulation and delivery of nutraceuticals, its ability to remove metal heavy ions has yet to be explored. In this study, for the first time, we demonstrated that the ferritin from kuruma prawns (Marsupenaeus japonicus), named MjF, has a pronouncedly larger ability to resist denaturation induced by Cd2+ and Hg2+ as compared to its analogue, human H-chain ferritin (HuHF), despite the fact that these two proteins share a high similarity in protein structure. Treatment of HuHF with Cd2+ or Hg2+ at a metal ion/protein shell ratio of 100/1 resulted in marked protein aggregation, while the MjF solution was kept constantly clear upon treatment with Cd2+ and Hg2+ at different protein shell/metal ion ratios (50/1, 100/1, 250/1, 500/1, 1000/1, and 2500/1). Structural comparison analyses in conjunction with the newly solved crystal structure of the complex of MjF plus Cd2+ or Hg2+ revealed that cysteine (Cys) is a major residue responsible for such binding, and that the large difference in the ability to resist denaturation induced by these two heavy metal ions between MjF and HuHF is mainly derived from the different positions of Cys residues in these two proteins; namely, Cys residues in HuHF are located on the outer surface, while Cys residues from MjF are buried within the protein shell. All of these findings raise the high possibility that prawn ferritin, as a food-derived protein, could be developed into a novel bio-template to remove heavy metal ions from contaminated food systems.

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9

Tzeng, Tzong-Der, Shean-Yeh Yeh, and Cho-Fat Hui. "Population genetic structure of the kuruma prawn (Penaeus japonicus) in East Asia inferred from mitochondrial DNA sequences." ICES Journal of Marine Science 61, no. 6 (January 1, 2004): 913–20. http://dx.doi.org/10.1016/j.icesjms.2004.06.015.

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Abstract Sequence analyses on the complete mitochondrial DNA (mtDNA) control region (992 bp) were conducted to elucidate the population structure of kuruma prawns (Penaeus japonicus) in East Asia. Five populations including 95 individuals were collected. They are separated into the Japan Sea (JS), the north and south of the East China Sea (NECS and SECS), the Taiwan Strait (TS), and the north of the South China Sea (NSCS) populations. There are 292 variable sites without any insertions and deletions. Nucleotide diversity in the total populations is 2.51 ± 0.07%, and the variations within populations ranged from 2.61 ± 0.93% (SECS) to 2.29 ± 0.16% (JS). FST values between the JS and the rest of the populations, between the NECS and NSCS populations, and between the SECS and NSCS populations show significant differences. The UPGMA tree of these five populations shows three distinct clusters; one includes the JS population; another includes the NECS population; the third includes populations from the rest of the areas. The analysis of molecular variance (AMOVA) shows clear genetic difference between the JS and the rest of the populations. Additional AMOVA analysis excluding the JS population indicates significant variation between the NECS population and the other three populations. We, therefore, conclude that three distinct populations exist in East Asia; one is in the JS; another is in the NECS; and the third is distributed in SECS, TS and NSCS.

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10

Kondo, Masakazu, Toshiaki Itami, Yukinori Takahashi, Reiko Fujii, and Susumu Tomonaga. "Phagocytes in the kidney of kuruma prawn." Developmental & Comparative Immunology 21, no. 1 (January 1997): 65. http://dx.doi.org/10.1016/s0145-305x(97)87957-8.

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11

Qiu, Gao-Feng, Hai-Yang Feng, and Keisuke Yamano. "Expression and Purification of Active Recombinant Cathepsin C (Dipeptidyl Aminopeptidase I) of Kuruma PrawnMarsupenaeus japonicusin Insect Cells." Journal of Biomedicine and Biotechnology 2009 (2009): 1–6. http://dx.doi.org/10.1155/2009/746289.

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Cathepsin C (CTSC) is a lysosomal cysteine protease belonging to the papain superfamily. Our previous study showed that CTSC precursor (zymogen) is localized exclusively in cortical rods (CRs) of mature oocyte in the kuruma prawnMarsupenaeus japonicus, suggesting that CTSC might have roles on regulating release and/or formation of a jelly layer. In this study, enzymically active CTSC of the kuruma prawn was prepared by recombinant expression in the High Five insect cell line. The recombinant enzyme with a polyhistidine tag at its C-terminus was considered to be initially secreted into the culture medium as an inactive form of zymogen, because Western blot with anti-CTSC antibody detected a 51 kDa protein corresponding to CTSC precursor. After purification by affinity chromatography on nickel-iminodiacetic acid resin, the enzyme displayed three forms of 51, 31, and 30 kDa polypeptides. All of the forms can be recognized by antiserum raised against C-terminal polyhistidine tag, indicating that the 31 and 30 kDa forms were generated from 51 kDa polypeptide by removal of a portion of the N-terminus of propeptide. Following activation at pH 5.5 and37∘Cfor 40 hours under native conditions, the recombinant CTSC (rCTSC) exhibited increased activity against the synthetic substrate Gly-Phe-β-naphthylamide and optimal pH at around 5. The purified rCTSC will be useful for further characterization of its exact physiological role on CRs release and/or formation of a jelly layer in kuruma prawn.

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12

Zhang, Heqian, Wenzhi Cheng, Jinbin Zheng, Panpan Wang, Qinghui Liu, Zhen Li, Tianyi Shi, Yijian Zhou, Yong Mao, and Xiangyong Yu. "Identification and Molecular Characterization of a Pellino Protein in Kuruma Prawn (Marsupenaeus Japonicus) in Response to White Spot Syndrome Virus and Vibrio Parahaemolyticus Infection." International Journal of Molecular Sciences 21, no. 4 (February 13, 2020): 1243. http://dx.doi.org/10.3390/ijms21041243.

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Kuruma prawn, Marsupenaeus japonicus, has the third largest annual yield among shrimp species with vital economic significance in China. White spot syndrome virus (WSSV) is a great threat to the global shrimp farming industry and results in high mortality. Pellino, a highly conserved E3 ubiquitin ligase, has been found to be an important modulator of the Toll-like receptor (TLR) signaling pathways that participate in the innate immune response and ubiquitination. In the present study, the Pellino gene from Marsupenaeus japonicus was identified. A qRT-PCR assay showed the presence of MjPellino in all the tested tissues and revealed that the transcript level of this gene was significantly upregulated in both the gills and hemocytes after challenge with WSSV and Vibrio parahaemolyticus. The function of MjPellino was further verified at the protein level. The results of the three-dimensional modeling and protein–protein docking analyses and a GST pull-down assay revealed that the MjPellino protein was able to bind to the WSSV envelope protein VP26. In addition, the knockdown of MjPellino in vivo significantly decreased the expression of MjAMPs. These results suggest that MjPellino might play an important role in the immune response of kuruma prawn.

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13

Mushiake, Keiichi, Misao Arimoto, Jun Satoh, and Koh-ichiro Mori. "Detection of PRDV from Wild Adult Kuruma Prawn." Fish Pathology 33, no. 5 (1998): 503–9. http://dx.doi.org/10.3147/jsfp.33.503.

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14

Nakamura, Kaworu. "Respiration of the Kuruma Prawn in Air Conditions." Fisheries science 60, no. 5 (1994): 621–22. http://dx.doi.org/10.2331/fishsci.60.621.

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15

Matsumoto, Misuzu, and Hideaki Yamanaka. "Studies on Rigor-Mortis of Kuruma Prawn Muscle." NIPPON SUISAN GAKKAISHI 57, no. 11 (1991): 2121–26. http://dx.doi.org/10.2331/suisan.57.2121.

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16

Yano, I. "Oocyte development in the kuruma prawn Penaeus japonicus." Marine Biology 99, no. 4 (November 1988): 547–53. http://dx.doi.org/10.1007/bf00392562.

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17

Vilella, Sebastiano, Vincenzo Zonno, Laura Ingrosso, Tiziano Verri, and Carlo Storelli. "Electroneutral Na+/H+exchange in brush-border membrane vesicles fromPenaeus japonicus hepatopancreas." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 274, no. 2 (February 1, 1998): R486—R493. http://dx.doi.org/10.1152/ajpregu.1998.274.2.r486.

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An electroneutral Na+/H+exchange mechanism (dimethylamiloride inhibitable, Li+ sensitive, and Ca2+ insensitive) was identified in brush-border membrane vesicles (BBMV) from Kuruma prawn hepatopancreas by monitoring Na+-dependent H+ fluxes with the pH-sensitive dye acridine orange and measuring22Na+uptake. Kinetic parameters measured under short-circuited conditions were the Na+ concentration that yielded one-half of the maximal dissipation rate ( F max) of the preset transmembrane ΔpH ( K Na) = 15 ± 2 mM and F max = 3,626 ± 197 Δ F ⋅ min−1 ⋅ mg protein−1, with a Hill coefficient for Na+ of ∼1. In addition, the inhibitory constant for dimethylamiloride was found to be ∼1 μM. The electroneutral nature of the antiporter was assessed in that an inside-negative transmembrane electrical potential neither affected kinetic parameters nor stimulated pH-dependent (intracellular pH > extracellular pH)22Na+uptake. In contrast, electrogenic pH-dependent22Na+uptake was observed in lobster hepatopancreatic BBMV. Substitution of chloride with gluconate resulted in increasing K Na and decreasing Δ F max, which suggests a possible role of chloride in the operational mechanism of the antiporter. These results indicate that a Na+/H+exchanger, resembling the electroneutral Na+/H+antiporter model, is present in hepatopancreatic BBMV from the Kuruma prawn Penaeus japonicus.

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18

Pena, Leobert D. de la, Hiroshi Koube, Toshihiro Nakai, and Kiyokuni Muroga. "Detection of Vibrio penaeicida in Kuruma Prawn after Transport." Fish Pathology 32, no. 4 (1997): 233–34. http://dx.doi.org/10.3147/jsfp.32.233.

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19

Kondo, Masakazu, Toshiaki Itami, Yukinori Takahashi, Reiko Fujii, and Susumu Tomonaga. "Ultrastructural and Cytochemical Characteristics of Phagocytes in Kuruma Prawn." Fish Pathology 33, no. 4 (1998): 421–27. http://dx.doi.org/10.3147/jsfp.33.421.

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20

Di Turi, L., M. Ragni, A. Vicenti, L. Melodia, and G. Vonghia. "Meat quality of Kuruma prawn (Marsupenaeus japonicus): preliminary evaluation." Italian Journal of Animal Science 4, sup2 (January 2005): 615–17. http://dx.doi.org/10.4081/ijas.2005.2s.615.

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21

SHIRAI, TAKAAKI, and YOSHIE KIKUCHI. "Extractive components of kuruma prawn Penaeus japonicus." Fisheries science 68, sup2 (2002): 1386–89. http://dx.doi.org/10.2331/fishsci.68.sup2_1386.

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22

Nakamura, Kaworu, and Yukinori Nishigaki. "Structure of Antennal Gland in Kuruma Prawn Penaeus japonicus." NIPPON SUISAN GAKKAISHI 57, no. 10 (1991): 1859–63. http://dx.doi.org/10.2331/suisan.57.1859.

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23

Nakamura, Kaworu, and Nobuhisa Nakashima. "Structure of Antennal Gland Coelomosac in the Kuruma Prawn." NIPPON SUISAN GAKKAISHI 58, no. 8 (1992): 1551. http://dx.doi.org/10.2331/suisan.58.1551.

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24

Wang, Hong Wei, Hai Ming Xu, Chun Long Zhao, Da Li, Hui Wang, and Duan Bo Cai. "Effects of Zinc on Hepatopancreatic Cell Culture of Kuruma Prawn, Litopenaeus vannamei." Advanced Materials Research 864-867 (December 2013): 151–54. http://dx.doi.org/10.4028/www.scientific.net/amr.864-867.151.

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The hepatopancreatic cell culture of the kuruma prawn, Litopenaeusvannamei, was conducted to identify the effects of zinc on cell division. The culturesystem consists of medium 199 (M 199) supplemented with 0.060 mol/L NaCl,1.011g/L glucose, 1000 UI/ml penicillin, 1000 μg/ml treptomycin, 20% heatinactivated fetal calf serum (FCS) for primary cells and 10 % for subculture cells. TheRNA/DNA ratio in cultured cells was measured. The results show that the celldivision of cultured hepatopancreas cells in L. vannamei was increased by the optimalconcentration of Zn2+, 80 μg/L.

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25

Wang, Hong Wei, Duan Bo Cai, Kai Ming Li, Hai Ming Xu, and Ming Duan. "Effects of Linoleic Acid on Hepatopancreatic Cell Proliferation of Prawn, Penaeus vannamei." Advanced Materials Research 403-408 (November 2011): 1368–70. http://dx.doi.org/10.4028/www.scientific.net/amr.403-408.1368.

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The effects of linoleic acid on hepatopancreatic cell culture of the kuruma prawn, Penaeus vannamei were conducted. The culture system consists of 199 media (M 199) supplemented with 0.060 mol/L NaCl, 1.011g/L glucose, 1000 UI/ml penicillin, 1000 μg/ml treptomycin, 20% heat inactivated fetal calf serum (FCS) for primary cells and 10 % for subculture cells. The content of phosphorus in cultured cells was measured. The results show that the growth condition of cultured hepatopancreas cells in P. vannamei was significantly improved by added 160 μmol/L linoleic acid.

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26

EGUSA, Syuzo, Yukinori TAKAHASHI, Toshiaki ITAMI, and Kazuo MOMOYAMA. "Histopathology of vibriosis in the Kuruma prawn, Penaeus japonicus BATE." Fish Pathology 23, no. 1 (1988): 59–65. http://dx.doi.org/10.3147/jsfp.23.59.

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27

Kondo, Masakazu, Toshiaki Itami, and Yukinori Takahashi. "Preliminary Characterization of Lectins in the Hemolymph of Kuruma Prawn." Fish Pathology 33, no. 4 (1998): 429–35. http://dx.doi.org/10.3147/jsfp.33.429.

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28

Yano, Isao. "Osmotic Concentration of Serum during Ovarian Maturation in kuruma Prawn." Fisheries science 61, no. 2 (1995): 349. http://dx.doi.org/10.2331/fishsci.61.349.

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29

Miyajima, Toshiaki, Yuichi Hamanaka, and Koji Toyota. "A Marking Method for Kuruma Prawn Penaeus japonicus." Fisheries science 65, no. 1 (1999): 31–35. http://dx.doi.org/10.2331/fishsci.65.31.

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30

IVITYADMA, TOSHIAKI, and KOJI TOYOTA. "A Marking Experiment for Kuruma Prawn Penaeus japonicus." Fisheries science 68, sup1 (2002): 900–903. http://dx.doi.org/10.2331/fishsci.68.sup1_900.

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31

Yamano, Keisuke, and Tatsuya Unuma. "Expressed sequence tags from eyestalk of kuruma prawn, Marsupenaeus japonicus." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 143, no. 2 (February 2006): 155–61. http://dx.doi.org/10.1016/j.cbpa.2005.11.005.

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32

FUSHIMI, HIROSHI. "5. Progress and future prospects on stock enhancement of Kuruma prawn." NIPPON SUISAN GAKKAISHI 81, no. 2 (2015): 301. http://dx.doi.org/10.2331/suisan.81.301.

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33

Mizuta, Shohshi, Reiji Yoshinaka, Mamoru Sato, and Morihiko Sakaguchi. "Hot-water Solubility of Collagen from the Muscle of Kuruma Prawn." Fisheries science 61, no. 3 (1995): 536–37. http://dx.doi.org/10.2331/fishsci.61.536.

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34

Nakajima, Hiroshi. "Natural mortality of Kuruma prawn in winter based on tagging experiments." NIPPON SUISAN GAKKAISHI 52, no. 10 (1986): 1759–64. http://dx.doi.org/10.2331/suisan.52.1759.

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35

Yoshikawa, Naoko. "Physiological Function of Free D-Alanine in Kuruma Prawn Marsupenaeus japonicus." Journal of The Society of Japanese Women Scientists 14, no. 1 (2014): 16–20. http://dx.doi.org/10.5939/sjws.14003.

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36

Yamano, Keisuke, Hisatake Seto, Gao-Feng Qiu, and Tatsuya Unuma. "Immunological characterization of cortical rod proteins of kuruma prawn, Marsupenaeus japonicus." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 136, no. 2 (October 2003): 371–77. http://dx.doi.org/10.1016/s1095-6433(03)00175-2.

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37

Nakamura, Kaworu, Takuji Okumura, and Katsumi Aida. "Identification of the Y Organ in the Kuruma Prawn Penaeus japonicus." NIPPON SUISAN GAKKAISHI 57, no. 8 (1991): 1463–68. http://dx.doi.org/10.2331/suisan.57.1463.

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38

Nakamura, Kaworu, Norikazu Matsuzaki, and Ken-Ichiroh Yonekura. "Organogenesis of Genital Organs and Androgenic Gland in the Kuruma Prawn." NIPPON SUISAN GAKKAISHI 58, no. 12 (1992): 2261–67. http://dx.doi.org/10.2331/suisan.58.2261.

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39

Li, Yutao, Keren Byrne, Emanuela Miggiano, Vicki Whan, Stephen Moore, Sandy Keys, Peter Crocos, Nigel Preston, and Sigrid Lehnert. "Genetic mapping of the kuruma prawn Penaeus japonicus using AFLP markers." Aquaculture 219, no. 1-4 (April 2003): 143–56. http://dx.doi.org/10.1016/s0044-8486(02)00355-1.

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40

Yoshikawa, N., S. Okada, and H. Abe. "Molecular Characterization of Alanine Racemase in the Kuruma Prawn Marsupenaeus japonicus." Journal of Biochemistry 145, no. 2 (November 13, 2008): 249–58. http://dx.doi.org/10.1093/jb/mvn162.

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41

Mohan, Chitradurga O., Chandraairi N. Ravishankar, Teralandur K. Srinivasa Gopal, and Jagannath Bindu. "Thermal processing of prawn ‘kuruma’ in retortable pouches and aluminium cans." International Journal of Food Science & Technology 43, no. 2 (January 24, 2008): 200–207. http://dx.doi.org/10.1111/j.1365-2621.2006.01369.x.

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42

Yoshinaka, Reiji, Shohshi Mizuta, Yoshiaki Itoh, and Mamoru Sato. "Two genetically distinct types of collagen in kuruma prawn Penaeus japonicus." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 96, no. 3 (January 1990): 451–56. http://dx.doi.org/10.1016/0305-0491(90)90038-u.

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43

Hamasaki, Katsuyuki, and Shuichi Kitada. "A review of kuruma prawn Penaeus japonicus stock enhancement in Japan." Fisheries Research 80, no. 1 (August 2006): 80–90. http://dx.doi.org/10.1016/j.fishres.2006.03.018.

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44

Benjakul, Soottawat, Wonnop Visessanguan, Tanong Aewsiri, and Munehiko Tanaka. "Dissociation of natural actomyosin from kuruma prawn muscle induced by pyrophosphate." Food Chemistry 102, no. 1 (January 2007): 295–301. http://dx.doi.org/10.1016/j.foodchem.2006.05.021.

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45

TAKAHASHI, Yukinori, Yasumasa SHIMOYAMA, and Kazuo MOMOYAMA. "Studies on the vibriosis of cultured kuruma prawn Peneaeus japonicus Bate. I. Pathogenicity and characteristics of Vibrio sp. isolated from cultured kuruma prawn Penaeus japonicus Bate." NIPPON SUISAN GAKKAISHI 51, no. 5 (1985): 721–30. http://dx.doi.org/10.2331/suisan.51.721.

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46

Pena, Leobert D. de la, Kazuo Momoyama, Toshihiro Nakai, and Kiyokuni Muroga. "Detection of the Causative Bacterium of Vibriosis in Kuruma Prawn, Penaeus japonicus." Fish Pathology 27, no. 4 (1992): 223–28. http://dx.doi.org/10.3147/jsfp.27.223.

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47

Satoh, Jun, Keiichi Mushiake, Koh-ichiro Mori, Misao Arimoto, Keinosuke Imaizumi, Toyohiko Nishizawa, and Kiyokuni Muroga. "Occurrence of PAV(Penaeid Acute Viremia) in Seed Production of Kuruma Prawn." Fish Pathology 34, no. 1 (1999): 33–38. http://dx.doi.org/10.3147/jsfp.34.33.

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48

Sakai, Takamitsu, Tatsumu Hirae, Kei Yuasa, Takashi Kamaishi, Tomomasa Matsuyama, Satoshi Miwa, Norihisa Oseko, and Takaji Iida. "Mass Mortality of Cultured Kuruma Prawn Penaeus japonicus Caused by Vibrio nigripulchritudo." Fish Pathology 42, no. 3 (2007): 141–47. http://dx.doi.org/10.3147/jsfp.42.141.

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49

Adachi, Kohsuke, Takashi Hirata, Katsunori Nagai, Satoshi Fujisawa, Masato Kinoshita, and Morihiko Sakaguchi. "Purification and Characterization of Prophenoloxidase from Kuruma Prawn Penaeus japonicus." Fisheries science 65, no. 6 (1999): 919–25. http://dx.doi.org/10.2331/fishsci.65.919.

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TSUTSUI, NAOAKI, ICHIRO KAWAZOE, TSUYOSHI OHIRA, SAFIAH JASMANI, WEI-JUN YANG, MARCY N. WILDER, and KATSUMI AIDA. "Vitellogenin of the kuruma prawn: the deduced primary structure and gene expression." Fisheries science 68, sup1 (2002): 973–74. http://dx.doi.org/10.2331/fishsci.68.sup1_973.

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