The estimation of anserinase activity by a low-temperature ninhydrin reaction
- 1 July 1959
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 72 (3) , 407-409
- https://doi.org/10.1042/bj0720407
Abstract
Anserine reacts negligibly slowly with ninhydrin reagent at 35[degree], whereas its component 1-methylhistidine and [beta]-alanine are reactive. This provides a basis for an improved colorimetric procedure for measuring low levels of hydrolysis of anserine.Keywords
This publication has 5 references indexed in Scilit:
- The free amino acids of fish. 1-Methylhistidine and β-alanine liberation by skeletal muscle anserinase of codling (Gadus callarias)Biochemical Journal, 1955
- PEPTIDASES IN HUMAN BLOOD .1. THE HYDROLYSIS OF GLYCYLGLYCINE AND GLYCYL-L-LEUCINE BY NORMAL SERUM1953
- A PHOTOMETRIC NINHYDRIN METHOD FOR THE MEASUREMENT OF PROTEOLYSISJournal of Biological Chemistry, 1950
- PHOTOMETRIC NINHYDRIN METHOD FOR USE IN THE CHROMATOGRAPHY OF AMINO ACIDSJournal of Biological Chemistry, 1948