Literature DB >> 19873167

ELECTROPHORESIS OF PEPSIN.

R M Herriott1, V Desreux, J H Northrop.   

Abstract

1. A number of pepsin solutions containing several protein components have been studied by the electrophoresis method. All samples show a homogeneous boundary moving to the anode at pH 4.4. 2. The activity of this material may be higher than that of the original solution on the basis of total nitrogen but is the same as that of the original solution on the basis of protein nitrogen. 3. There is no separation of the various protein components under these conditions. 4. The apparent isoelectric point at pH 2.7, previously obtained by the collodion particle method is due to the presence of decomposition products. Pure crystalline pepsin, free from decomposition products, is always negatively charged.

Entities:  

Year:  1940        PMID: 19873167      PMCID: PMC2237938          DOI: 10.1085/jgp.23.4.439

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


  4 in total

1.  Electrophoresis of pepsin.

Authors:  A Tiselius; G E Henschen; H Svensson
Journal:  Biochem J       Date:  1938-10       Impact factor: 3.857

2.  A TEST FOR DIFFUSIBLE IONS : II. THE IONIC NATURE OF PEPSIN.

Authors:  J H Northrop
Journal:  J Gen Physiol       Date:  1925-05-20       Impact factor: 4.086

3.  THE PRESENCE OF A GELATIN-LIQUEFYING ENZYME IN CRUDE PEPSIN PREPARATIONS.

Authors:  J H Northrop
Journal:  J Gen Physiol       Date:  1931-09-20       Impact factor: 4.086

4.  CRYSTALLINE PEPSIN : IV. HYDROLYSIS AND INACTIVATION BY ACID.

Authors:  J H Northrop
Journal:  J Gen Physiol       Date:  1932-09-20       Impact factor: 4.086

  4 in total
  1 in total

1.  QCM-based assay designs for human serum albumin.

Authors:  Wisnu Arfian A Sudjarwo; Mathias Thomas Dobler; Peter A Lieberzeit
Journal:  Anal Bioanal Chem       Date:  2021-12-23       Impact factor: 4.142

  1 in total

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