Literature DB >> 19075

Enhanced heat, alkaline and tryptic stability of acetamidinated pig heart lactate dehydrogenase.

P Tuengler, G Pfleiderer.   

Abstract

Modification of 17 from 24 lysine residues in pig heart lactate dehydrogenase (L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) with methyl aceimidate yields an enzyme derivative with enhanced stability toward meat and alkaline denaturation as well as tryptic digestion. The specific activity of the modified enzyme is only slightly reduced

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Year:  1977        PMID: 19075     DOI: 10.1016/0005-2744(77)90108-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

Review 1.  Enzyme stabilization: state of the art.

Authors:  L Gianfreda; M R Scarfi
Journal:  Mol Cell Biochem       Date:  1991-02-02       Impact factor: 3.396

2.  [Lactate dehydrogenase. An example of the development of modern enzymology].

Authors:  G Pfleiderer
Journal:  Naturwissenschaften       Date:  1978-08

3.  Arginyl residues and thermal stability in proteins.

Authors:  F S Qaw; J M Brewer
Journal:  Mol Cell Biochem       Date:  1986-08       Impact factor: 3.396

  3 in total

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