Literature DB >> 4311027

Equilibrium and kinetic studies on the reversible dissociation of yeast enolase by neutral salts.

T H Gawronski, E W Westhead.   

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Year:  1969        PMID： 4311027     DOI： 10.1021/bi00839a006

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  3 in total

1.  Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model.

Authors:  Dénison S Sánchez-Miguel; Jahir Romero-Jiménez; César A Reyes-López; Ana Lilia Cabrera-Avila; Normande Carrillo-Ibarra; Claudia G Benítez-Cardoza
Journal:  Protein J       Date:  2010-01       Impact factor: 2.371

2.  Kinetic and spectroscopic evidence of cation-induced conformation changes in yeast K+ -activated aldehyde dehydrogenase.

Authors:  G F Betts; P L Poole; M G Springham; K A Bostian
Journal:  Biochem J       Date:  1979-12-01       Impact factor: 3.857

3.  Refolding of triose phosphate isomerase.

Authors:  S G Waley
Journal:  Biochem J       Date:  1973-09       Impact factor: 3.857
  3 in total

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