[Preliminary studies on transaminase of Oncomelania snail]

Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi. 1990;8(2):110-2.
[Article in Chinese]

Abstract

By paper chromatography, the tissue homogenate of Oncomelania snails was shown to form glutamic acid at the expense of alpha-ketoglutarate plus aspartic acid, alanine or arginine respectively. The existence of alanine-glutamate, aspartate-glutamate and arginine-glutamate transaminase in Oncomelania snail was demonstrated. By using colorimetric method, the activity of aspartate-glutamate transaminase (GOT) and alanine-glutamate transaminase (GPT) of Oncomelania snail was 1.64 +/- 0.01 and 0.99 +/- 0.01 mumol/h.mg protein respectively. GOT and GPT were not inhibited by 2 ppm bromoacetamide, but the activity of GPT was suppressed (40%) by 2 ppm nicotinanilide. A combination of 0.5 ppm bromoacetamide and 0.5 ppm nicotinanilide had no synergitic molluscicidal effect.

Publication types

  • English Abstract

MeSH terms

  • Acetamides / pharmacology
  • Alanine Transaminase / metabolism*
  • Animals
  • Aspartate Aminotransferases / metabolism*
  • Molluscacides / pharmacology
  • Nicotinic Acids / pharmacology
  • Snails / enzymology*

Substances

  • Acetamides
  • Molluscacides
  • Nicotinic Acids
  • N-bromoacetamide
  • nicotinanilide
  • Aspartate Aminotransferases
  • Alanine Transaminase