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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

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: 745 *