The hemolymph clottable proteins of tiger shrimp, Penaeus monodon, and related species

Maw Sheng Yeh, Yuh Ling Chen, Inn Ho Tsai

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47 Citations (Scopus)


A clottable protein was purified from the hemolymph of tiger shrimp (Penaeus monodon) by sequential DEAE anion-exchange chromatography. The protein formed stable clots in the presence of Ca2+ and the transglutaminase in hemocyte lysate. It is thermostable at temperatures up to 66°C. The molecular mass of the clottable protein was determined to be 380 kDa by SDS-PAGE and MALDI-TOF mass spectrometry, and the protein exists as disulfide-linked homodimers and oligomers. The size and amino acid composition of the clottable protein are similar to those of several other shrimps, prawns, lobster and crayfish, and their N-terminal amino acid sequences are 60-80% identical. Monosaccharide analysis of the clottable protein revealed the presence of mannose, glucosamine or N-acetylglucosamine and possibly glucose in this glycoprotein of about 5% sugar content. Lipid in the protein upon electrophoresis was hardly detectable with the Oil Red O staining method. In immunodiffusion and immunoblotting analyses, the anti-clottable protein antibodies reacted with the clottable proteins from the penaeid shrimps but not with those from other crustaceans. Copyright (C) 1998 Elsevier Science Inc.

Original languageEnglish
Pages (from-to)169-176
Number of pages8
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number2
Publication statusPublished - 1998 Dec 1

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

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