Crystallization of the fungal enzyme proteinase K and amino acid composition
1975; Elsevier BV; Volume: 97; Issue: 2 Linguagem: Inglês
10.1016/s0022-2836(75)80039-8
ISSN1089-8638
AutoresJ. Κ. Dattagupta, Takashi Fujiwara, E. V. Grishin, Klaus Lindner, Philip C. Manor, Norman J. Pieniążek, Wolfram Saenger, Dietrich Suck,
Tópico(s)Porphyrin Metabolism and Disorders
ResumoProteinase K is obtained from the fungus Tritirachium album Limber and is named after its keratin-digesting activity. The enzyme, of molecular weight 18,500, is a serine proteinase and hydrolyses proteins at the carboxyl end of hydrophobic amino acids, as does α-chymotrypsin. The amino acid composition of proteinase K was determined by standard methods and the protein was crystallized using an improved dialysis method. The crystals obtained have been characterized by X-ray diffraction methods; the space group is tetragonal, P41212 or P43212 and the cell constants are a = b = 68·3 Å, c = 108·5 Å; two protein molecules are found in one asymmetric unit.
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