Literature DB >> 16745028

The hydrolysis of caseinogen by pepsin and by trypsin-kinase.

J D Stirling1, G M Wishart.   

Abstract

Year:  1932        PMID: 16745028      PMCID: PMC1261128          DOI: 10.1042/bj0261989

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


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  2 in total

1.  Some Phosphorus Compounds of Milk: The Liberation of Phosphorus from Caseinogen by Enzymes and other Agents.

Authors:  C Rimington; H D Kay
Journal:  Biochem J       Date:  1926       Impact factor: 3.857

2.  Some Phosphorus Compounds of Milk. III: Dephosphorised Caseinogen. The Action of Alkali upon Caseinogen.

Authors:  C Rimington
Journal:  Biochem J       Date:  1927       Impact factor: 3.857

  2 in total
  5 in total

1.  The conversion of casein into microbial proteins in the rumen.

Authors:  I W McDONALD; R J HALL
Journal:  Biochem J       Date:  1957-11       Impact factor: 3.857

2.  The heat-coagulation of caseinogen: The rôle of phosphorus cleavage.

Authors:  G R Howat; N C Wright
Journal:  Biochem J       Date:  1934       Impact factor: 3.857

3.  The nature of paranuclein: A comparison of the peptic digestion products of various phosphoproteins.

Authors:  J D Herd
Journal:  Biochem J       Date:  1937-09       Impact factor: 3.857

4.  The hydrolysis of lecitho-vitellin by pepsin and by trypsin-kinase.

Authors:  J H Blackwood; G M Wishart
Journal:  Biochem J       Date:  1934       Impact factor: 3.857

5.  The nature of paranuclein.

Authors:  J D Herd
Journal:  Biochem J       Date:  1936-09       Impact factor: 3.857

  5 in total

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