Separation of the proteolytic and esterasic activities of trypsin by reversible structural modifications.

Coletti-Previero, M A; Previero, A; Zuckerkandl, E

Coletti-Previero, M A; Previero, A; Zuckerkandl, E.

J Mol Biol ; 39(3): 493-501, 1969 Feb 14.

Article in En | MEDLINE | ID: mdl-5390558

Subject(s)

Trypsin; Amino Acid Sequence; Animals; Caseins; Cattle; Dioxins; Endopeptidases; Esterases; Ethanol; Formamides; Formates; Hydrogen-Ion Concentration; Solvents; Spectrophotometry; Tryptophan; Ultraviolet Rays

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Collection: 01-internacional Database: MEDLINE Main subject: Trypsin Limits: Animals Language: En Journal: J Mol Biol Year: 1969 Type: Article

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PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Trypsin Limits: Animals Language: En Journal: J Mol Biol Year: 1969 Type: Article