Literature DB >> 13834525

The denaturation of ovalbumin. Changes in optical rotation, extinction and viscosity during serial denaturation in solutions of urea.

F S STEVEN, G R TRISTRAM.   

Abstract

Entities:  

Keywords:  EGG WHITE/chemistry; UREA/pharmacology

Mesh:

Substances:

Year:  1959        PMID: 13834525      PMCID: PMC1197016          DOI: 10.1042/bj0730086

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


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  4 in total

1.  The reactivity of free amino groups in native and denatured ovalbumin towards fluorodinitrobenzene.

Authors:  F S STEVEN; G R TRISTRAM
Journal:  Biochem J       Date:  1958-10       Impact factor: 3.857

2.  Protein structure in relation to function and biosynthesis.

Authors:  C B ANFINSEN; R R REDFIELD
Journal:  Adv Protein Chem       Date:  1956

3.  Liberation of tyrosine hydroxyl groups in urea solutions of bovine serum albumin and ovalbumin.

Authors:  A N GLAZER; H A McKENZIE; R G WAKE
Journal:  Nature       Date:  1957-12-07       Impact factor: 49.962

4.  The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration.

Authors:  J L Crammer; A Neuberger
Journal:  Biochem J       Date:  1943-07       Impact factor: 3.857

  4 in total
  3 in total

1.  The denaturation of acetic acid-soluble calf-skin collagen. Changes in optical rotation, viscosity and susceptibility towards enzymes during serial denaturation in solutions of urea.

Authors:  F S STEVEN; G R TRISTRAM
Journal:  Biochem J       Date:  1962-10       Impact factor: 3.857

2.  The relative stabilities of the skeletal-muscle myosins of some animals.

Authors:  J J CONNELL
Journal:  Biochem J       Date:  1961-09       Impact factor: 3.857

3.  Studies of the denaturation and partial renaturation of ovalbumin.

Authors:  J C Holt; J M Creeth
Journal:  Biochem J       Date:  1972-09       Impact factor: 3.857

  3 in total

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