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A protease from Astacus fluviatilis as an aid in protein sequencing

✍ Scribed by Erika Krauhs; Herbert Dörsam; Melvyn Little; Robert Zwilling; Herwig Ponstingl

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
359 KB
Volume
119
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis

A protease from the digestive tract of the crayfish Astacus jluviatilis (EC 3.4.99.6), which does not seem to belong to any of the known families of proteases, proves to be a valuable aid in sequencing proteins. In denatured polypeptide chains, it has the unusual property of hydrolyzing peptide bonds on the amino side of the small uncharged residues Ala, Thr, Ser, Gly, and Val. The number of cleavage sites, however, is restricted to about one-fifth of the respective residues present. A requirement for cleavage may be the capability of the polypeptide chain to assume a conformation similar to a reverse turn at the site of hydrolysis.

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