Biomaterial Database

Human proinsulin, IV[1--3]: synthesis of a protected peptide fragment corresponding to the sequence 1--23 of the prohormone. 1980

W Danho, and J Föhles

The synthesis of the protected peptide fragment: Boc-Phe-Val-Asn-Gln-His-Leu-Cys-(Trt)-Gly-Ser(But)-His-Leu-Val-Glu(OBut)-Ala-Le u-Tyr(But)-Leu-Val-Cys(Trt)-Gly-Glu(OBut)-Arg(HCl)-Gly-OH, corresponding to the sequence 1--23 of human proinsulin (sequence 1--23 of human insulin B chain) is described. The fragment was synthesized from two intermediate fragments: 1--16 and 17--23 and was purified by gel filtrationon Sephadex LH-20 in dimethylformamide.

UI	MeSH Term	Description	Entries
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011384	Proinsulin	A pancreatic polypeptide of about 110 amino acids, depending on the species, that is the precursor of insulin. Proinsulin, produced by the PANCREATIC BETA CELLS, is comprised sequentially of the N-terminal B-chain, the proteolytically removable connecting C-peptide, and the C-terminal A-chain. It also contains three disulfide bonds, two between A-chain and B-chain. After cleavage at two locations, insulin and C-peptide are the secreted products. Intact proinsulin with low bioactivity also is secreted in small amounts.
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein