Literature DB >> 3468505

Thermal and pH stability of "beta-benzyme".

V T D'Souza, X L Lu, R D Ginger, M L Bender.   

Abstract

The thermal and pH stability of "beta-benzyme", an artificial chymotrypsin based on beta-cyclodextrin, has been studied and compared with the stability of real chymotrypsin. Artificial chymotrypsin is vastly superior to real chymotrypsin with regard to both temperature and pH stability. The reasons for this increased stability are discussed.

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Year:  1987        PMID： 3468505      PMCID： PMC304277          DOI： 10.1073/pnas.84.3.673

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  4 in total

1.  Elimination of cannibalistic denaturation by enzyme immobilization or inhibition.

Authors:  H L Wu; D A Lace; M L Bender
Journal:  Proc Natl Acad Sci U S A       Date:  1981-07       Impact factor: 11.205

2.  Ageing of alpha-chymotrypsin: Cannibalistic and hydroxide ion reactions.

Authors:  H L Wu; A Wastell; M L Bender
Journal:  Proc Natl Acad Sci U S A       Date:  1981-07       Impact factor: 11.205

3.  Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level.

Authors:  H K Schachman; S J Edelstein
Journal:  Biochemistry       Date:  1966-08       Impact factor: 3.162

4.  Structure of alpha-chymotrypsin refined at 1.68 A resolution.

Authors:  H Tsukada; D M Blow
Journal:  J Mol Biol       Date:  1985-08-20       Impact factor: 5.469
  4 in total
  1 in total

Review 1.  Arac/XylS family of transcriptional regulators.

Authors:  M T Gallegos; R Schleif; A Bairoch; K Hofmann; J L Ramos
Journal:  Microbiol Mol Biol Rev       Date:  1997-12       Impact factor: 11.056
  1 in total

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