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Preparation of Des-alanine-B30-insulin via the Tryptic Hydrolysis of Porcine Insulin Modified at the Arginyl Residue by Cyclohexane-1,2-dione

B. Mulac ; Tracer Laboratory, Department of Organic Chemistry and Biochemistry, »Ruder Boskovic« Institute, POB 1016, 41001 Zagreb, Croatia, Yugoslavia
D. Keglević ; Tracer Laboratory, Department of Organic Chemistry and Biochemistry, »Ruder Boskovic« Institute, POB 1016, 41001 Zagreb, Croatia, Yugoslavia


Puni tekst: engleski pdf 4.480 Kb

str. 107-113

preuzimanja: 223

citiraj


Sažetak

The feasibility of the selective modification of the argimyl residue
in insulin by the method of Patthy and Smith (J. Biol. Chem.
250 (1975) 557-564; ibid. 565-569), involving the reversible reaction
of cyclohexane-1,2-dicme wiith the guanidrinio function of arginine in
a borate buffer, was studied. It was found that cyclohexane-1,2-
-di,one reacts specifically and completely Wli.th the arginyl residue of
porcine insulin in 0.2 M borate buffer at pH = 9.0 to form a single
addition product ([DHCH-Arg-B22]-insulin complex I) which, upon
treatment with 0.5 M hydroxylamine at pH = 7.0, regenerated
insulin of unchanged biological activity. Incubation of I with
trypsin led to specific cleavage at the Lys-B29 residue to give des-
Ala-B30-[DHCH-Arg-B22]-insulin complex II, which, upon hydroxylamine
treatment afforded des-Ala-B30-insulin (III) in high yield.

Ključne riječi

Hrčak ID:

194621

URI

https://hrcak.srce.hr/194621

Datum izdavanja:

5.5.1980.

Posjeta: 490 *