Biomaterial Database

Human pancreatic proelastase 2. Sequence of the activation peptide. 1980

C Largman, and J W Brodrick, and M C Geokas

The N-terminal sixteen residues of the amino acid sequence of reduced and alkylated human pancreatic proelastase 2 have been established, and N-terminal amino acid residue has been shown to be carboxymethylcysteine. A peptide containing an amino acid sequence corresponding to the first twelve residues of proelastase 2 was isolated following activation of proelastase 2 with trypsin, performic acid oxidation, and gel filtration. This peptide was not released prior to performic acid oxidation, suggesting that it remains attached to the major peptide chain via a disulfide bond containing the N-terminal half-cysteine in a manner similar to that found for chymotrypsinogens. However, the amino acid sequence of the activation peptide is not strongly homologous to either porcine chymotrypsinogen A or porcine proelastase 1.

UI	MeSH Term	Description	Entries
D010179	Pancreas	A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
D010196	Pancreatic Elastase	A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.	Elastase,Pancreatopeptidase,Elastase I,Pancreatic Elastase I,Elastase I, Pancreatic,Elastase, Pancreatic
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D004789	Enzyme Activation	Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.	Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D004792	Enzyme Precursors	Physiologically inactive substances that can be converted to active enzymes.	Enzyme Precursor,Proenzyme,Proenzymes,Zymogen,Zymogens,Precursor, Enzyme,Precursors, Enzyme
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