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Digestion of matrix-bound camel insulin with pepsin was found to be restricted to the cleavage of the peptide bond between phenylalanine(B25) and tyrosine(B26). Purification of the camel des-pentapeptide(B26-30)-insulin obtained was achieved by gel filtration and ion exchange chromatography, yielding a molecularly uniform product. In the same way, camel des-PheB1-insulin prepared according to a method described for bovine insulin was hydrolyzed with pepsin and purified to give the des-PheB1-despentapeptide(B26-30)-insulin. The biological activity of these modified camel insulins was found to be as much reduced as the corresponding bovine insulin analogues. However, the reduced biological activity of camel des-PheB1-insulin (60%) was a contrast to the fully active bovine des-PheB1-insulin.
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
September 1975,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1972,
Biokhimiia (Moscow, Russia),
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1976,
Scientia Sinica,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1976,
Scientia Sinica,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1976,
Scientia Sinica,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1979,
International journal of peptide and protein research,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1976,
Scientia Sinica,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
June 1969,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
March 1987,
Biological chemistry Hoppe-Seyler,
W O Danho, and
H G Gattner, and
D Nissen, and
H Zahn
January 1995,
International journal of peptide and protein research,
