ISSN:
1435-1536
Schlagwort(e):
Chymotrypsinogen
;
chymotrypsin fragments
;
CD
;
secondary structure
;
sodiumdodecylsulfate
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Chemie und Pharmazie
,
Maschinenbau
Notizen:
Abstract Secondary structural changes of chymotrypsinogen A,α-chymotrypsin, and their isolated polypeptides Cys1-Leu13, Ile16-Tyr146, and Ala149-Asn245were examined in aqueous solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride (residue numbers from chymotrypsinogen). After the fragmentation by the cleavage of disulfide bridges inα-chymotrypsin, the helical structure was formed in the isolated polypeptide 16–146 where the helical segments do not exist in the protein state. The polypeptide 149–245, where the helical segments of the parent protein are originally located, contained no helices. The polypeptide 1–13 was almost disordered. The three polypeptides, chymotrypsinogen,α-chymotrypsin and the polypeptide 16–146, clearly showed differences in the stabilities of helical structures in solutions of urea and guanidine hydrochloride. The addition of SDS accelerated the formation of helical structures in each polypeptide except for 1–13.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF01410401
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