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Biomedical subjects

M Samel

Publications and source records attributed to M Samel.

4 recordsLinked to original sources
PubMed1990

Isolation and characterization of hemorrhagic metalloproteinase from Vipera berus berus (common viper) venom.

1. Hemorrhagic metalloproteinase (HMP) was isolated by gel filtration on a Sephadex G-100 (superfine) and affinity chromatography on agarose HPS-7. 2. Hemorrhagic metalloproteinase is a glycoprotein with mol. wt 56.3 kDa. It contains 1 zinc atom per molecule of protein. 3. Hemorrhagic metalloproteinase hydrolyzes casein, fibrinogen and splits the insulin B chain at positions Ala14-Leu15, Tyr16-Leu17, His10-Leu11. It digests A alpha chain of fibrinogen.

Amino Acid Sequence↗
PubMed1987

Purification and characterization of two arginine ester hydrolases from Vipera berus berus (common viper) venom.

Two arginine ester hydrolases, designated EI and EII, consist of multiple molecular forms with pI values in the range 4.0-4.6 for EI and 3.3-3.9 for EII. Isoforms had identical molecular weights: 38,500 for EI and 41,000 for EII (SDS electrophoresis). The N-terminal amino acid for both enzymes was valine and their amino acid contents were very similar, with both containing carbohydrate. After treatment of EI and EII with neuraminidase both enzymes migrated identically in the electrofocusing system. Neither esterase hydrolyzed casein, alpha-N-benzoyl-DL-arginine-p-nitroanilide (BAPNA), yet both hydrolyzed alpha-N-benzoyl-L-arginine methylester (BAEE), p-tosyl-L-arginine methylester (TAME) and Pro-Phe-Arg-MCA. The esterase activities of the two enzymes were inhibited by organophosphorus inhibitors and benzamidine. The Km value for EI with BAEE was 3.3 X 10(-5) M, with TAME 3.0 X 10(-5) M, and for EII 2.7 X 10(-5) M (BAEE) and 5.9 X 10(-5) M (TAME). EII possessed kinin-releasing activity, as shown by the twitch response of an isolated rat uterus. The physiological role of EI is unknown. Neither esterase has thrombin-like or fibrionlytic activities.

Amino Acids↗
PubMed1986

Isolation and characterization of nerve growth factor from Vipera berus berus (common viper) venom.

Nerve growth factor from Vipera berus berus venom was purified by gel filtration on Sephadex G-100 (superfine), ion-exchange-chromatography on DEAE-Sephadex A-50 and chromatofocusing on PBE 118. The Vipera berus berus venom NGF consists of multiple molecular forms with pls in the interval 9.1-9.7. All isoforms have identical mol. wts approximately 35,000 +/- 3000 (in gel filtration) and 17,000 +/- 2000, 15,000 +/- 2000 (by SDS electrophoresis with beta-mercaptethanol). V. berus berus venom NGF reacted with monoclonal antibodies against Viper lebetina NGF and caused differentiation of pheochromocytoma PC12 cells.

Animals↗