Biomaterial Database

Simultaneous formation of native ribonuclease and proinsulin from their mixed S-sulfonated derivatives by protein disulfide isomerase. 1992

X C Yu, and C L Tsou

National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.

Although the formation of native disulfide bonds of a protein from randomly linked disulfides by protein disulfide isomerase has been extensively studied, the possibility of simultaneous formation of the native proteins from a mixture has not been examined. It is shown in this paper that native ribonuclease and proinsulin can be nearly quantitatively formed by protein disulfide isomerase from a mixture of their S-sulfonated derivatives independent of the presence of each other.

UI	MeSH Term	Description	Entries
D007535	Isomerases	A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.	Isomerase
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.
D004229	Dithiothreitol	A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.	Cleland Reagent,Cleland's Reagent,Sputolysin,Clelands Reagent,Reagent, Cleland,Reagent, Cleland's
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012260	Ribonucleases	Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.	Nucleases, RNA,RNase,Acid Ribonuclease,Alkaline Ribonuclease,Ribonuclease,RNA Nucleases,Ribonuclease, Acid,Ribonuclease, Alkaline
D013431	Sulfates	Inorganic salts of sulfuric acid.	Sulfate,Sulfates, Inorganic,Inorganic Sulfates
D019704	Protein Disulfide-Isomerases	Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.	Protein Disulfide Isomerase,Protein Disulfide-Isomerase,Disulfide Interchange Enzyme,Disulfide Isomerase,Glycosylation Site-Binding Protein,Sulfhydryl-Disulfide Interchange Enzyme,Thiol-Disulfide Transhydrogenase,Trypanothione-Glutathione Thioltransferase,Disulfide Isomerase, Protein,Disulfide-Isomerase, Protein,Disulfide-Isomerases, Protein,Enzyme, Disulfide Interchange,Enzyme, Sulfhydryl-Disulfide Interchange,Glycosylation Site Binding Protein,Interchange Enzyme, Disulfide,Interchange Enzyme, Sulfhydryl-Disulfide,Isomerase, Disulfide,Isomerase, Protein Disulfide,Protein Disulfide Isomerases,Protein, Glycosylation Site-Binding,Site-Binding Protein, Glycosylation,Sulfhydryl Disulfide Interchange Enzyme,Thiol Disulfide Transhydrogenase,Thioltransferase, Trypanothione-Glutathione,Transhydrogenase, Thiol-Disulfide,Trypanothione Glutathione Thioltransferase