Literature DB >> 19872789

THE EQUILIBRIUM BETWEEN ACTIVE NATIVE TRYPSIN AND INACTIVE DENATURED TRYPSIN.

M L Anson1, A E Mirsky.   

Abstract

There is a mobile equilibrium between the native and denatured forms of trypsin which depends on the concentrations of acid, alkali, and alcohol and on the temperature. The heat of denaturation in 0.01 N hydrochloric acid calculated from the effect of temperature on the equilibrium constant is -67,600 calories per mole.

Entities:  

Year:  1934        PMID: 19872789      PMCID: PMC2141297          DOI: 10.1085/jgp.17.3.393

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


  4 in total

1.  Equilibrium constants and free energies in unfolding of proteins in urea solutions.

Authors:  I M Klotz
Journal:  Proc Natl Acad Sci U S A       Date:  1996-12-10       Impact factor: 11.205

2.  [Not Available].

Authors:  P RONDONI
Journal:  Experientia       Date:  1946-04-15

3.  Elastin fragment-induced monocyte chemotaxis. The role of desmosines.

Authors:  M Kunitomo; M Jay
Journal:  Inflammation       Date:  1985-06       Impact factor: 4.092

4.  Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus.

Authors:  Marianne A Grant; Noel D Lazo; Aleksey Lomakin; Margaret M Condron; Hiromi Arai; Ghiam Yamin; Alan C Rigby; David B Teplow
Journal:  Proc Natl Acad Sci U S A       Date:  2007-10-10       Impact factor: 11.205

  4 in total

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