1982

DOI: 10.1016/0160-9327(82)90069-2

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Insulin chemistry—pathway to understanding insulin action

Dietrich Brandenburg²,

Shang-chuan Chu³

et al.

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Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung

Kuhl²,

1985

Angewandte Chemie

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Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung

Kuhl²,

1985

Angewandte Chemie

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Basic Principles of Protease‐Catalyzed Peptide Bond Formation

¹

,

²

,

³

1985

Angew. Chem. Int. Ed. Engl.

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The stereospecific formation of peptide bonds under mild conditions and without side reactions is still a formidable task in peptide synthesis. One approach that springs to mind, namely the use of the naturally occurring catalyst involved in the biosynthesis of proteins, the ribosomal peptidyl transferase, cannot be realized in practice. The fact, however, that the natural cleavage of proteins is carried out by other enzymes, namely the proteases, together with the reversibility of these cleavage reactions in principle, has led to an interesting synthetic concept. Proteases normally catalyze the enzymatic degradation of proteins and peptides by hydrolytic cleavage of the peptide bond in an exergonic reaction. The use of physicochemical principles in order to influence the equilibrium, the concentration of products, and the kinetic parameters of the reaction results in the successful application of the catalytic properties of proteases to peptide synthesis. The purpose of this review is to describe and summarize the methods used in such approaches and to attempt a systematic categorization. The principles are applied to the synthesis of such practically relevant products as aspartame and human insulin.

Effects of modified insulin B21-B26 fragments on glycogenesis and on insulin-receptor complex fate in cultured fetal hepatocytes

Plas²,

1989

Molecular and Cellular Endocrinology

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