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Kallikrein-like enzyme from Crotalus ruber ruber (red rattlesnake) venom by Nobuhiro Mori; Hisayoshi Sugihara is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A~tract--1. A kallikrein-like enzyme was isolated and characterized from the venom of Crotalus ruber tuber (red rattlesnake). 2. The kallikrein-like enzyme was shown to be homogeneous as demonstrated by a single band on acrylamide gel electrophoresis, isoelectric focusing, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunodiffusion and reverse-phase (RP) HPLC. 3. The enzyme has a molecular weight of 31,000 and isoelectric point of 4.6. It consists of 271 total amino acid residues, 24% of which are acidic amino acids. 4. Specific esterolytic activities of the kallikrein-like enzyme on N-tosyl-L-arginine methylester (TAME) and N-benzoyl-L-arginine ethylester (BAEE) are 109.5 and 23.6/~mol/min/mg, respectively. 5. The enzyme differs from trypsin as the soybean trypsin inhibitor does not inhibit the enzyme's action. Diisopropylfluorophosphate (DFP) inhibits the enzyme, suggesting that the serine hydroxyl group is important for enzyme activity. 6. The enzyme is not lethal at 15/~g/g in mice and has no hemorrhagic activity, yet the injection of the purified enzyme intradermally, produced capillary permeability-increasing activity as shown by the use of Evans blue dye, and

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Author

Nobuhiro Mori; Hisayoshi Sugihara

Publisher

Elsevier Science; Elsevier ; Pergamon Press Ltd.; Elsevier BV (ISSN 0020-711X)

Published

1988

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)