Literature DB >> 19872688

CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID.

J H Northrop1.   

Abstract

The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45 degrees C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were continued until less than 5 per cent of the original protein remained. These results indicate that none of the split products of the protein molecule possess any appreciable activity compared to that of the original protein.

Entities:  

Year:  1932        PMID: 19872688      PMCID: PMC2323772          DOI: 10.1085/jgp.16.1.33

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  2 in total

1.  [The influence of time and temperature on the digestive effect of human gastric juice of varying peptic activity and pH concentration on living tissue. II. Spectrometric findings in digestion of frog legs].

Authors:  R M Konrad; F Sadra
Journal:  Langenbecks Arch Chir       Date:  1969-04-28

2.  ELECTROPHORESIS OF PEPSIN.

Authors:  R M Herriott; V Desreux; J H Northrop
Journal:  J Gen Physiol       Date:  1940-03-20       Impact factor: 4.086

  2 in total

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