Biomaterial Database

Amino acid sequence analysis of the asparagine-288 region of the carbohydrate variants of human plasminogen. 1983

J R Powell, and F J Castellino

The amino acid sequences of the two major carbohydrate variants in the region of Asn288 have been determined. A peptide isolated from plasminogen variant 1, which contains a complex-type Asn288-linked oligosaccharide, was found to possess the amino acid sequence-Ser280-Ala-Gln-Thr-Pro-His-Thr-His-Asn(CHO)-Arg-Thr290-Pro-Glu-, in agreement with the previously published sequence [Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T. E., & Magnusson, S. (1978) in Progress in Chemical Fibrinolysis and Thrombolysis (Davidson, J. F., Rowan, R. M., Samama, M. M., & Desnoyers, P. C., Eds.) Vol. 3, pp 191-209, Raven Press, New York]. A similar peptide isolated from plasminogen variant 2 did not contain oligosaccharide but possessed an amino acid sequence identical with the corresponding variant 1 peptide. Thus, the basis for the lack of the complex-type oligosaccharide in human plasminogen variant 2 does not reside in substitution of essential amino acid residues in the region of the Asn288-linked glycosylation site.

UI	MeSH Term	Description	Entries
D009844	Oligosaccharides	Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.	Oligosaccharide
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010958	Plasminogen	Precursor of plasmin (FIBRINOLYSIN). It is a single-chain beta-globulin of molecular weight 80-90,000 found mostly in association with fibrinogen in plasma; plasminogen activators change it to fibrinolysin. It is used in wound debriding and has been investigated as a thrombolytic agent.	Profibrinolysin,Glu-Plasminogen,Glutamic Acid 1-Plasminogen,Glutamyl Plasminogen,1-Plasminogen, Glutamic Acid,Glu Plasminogen,Glutamic Acid 1 Plasminogen,Plasminogen, Glutamyl
D002268	Carboxypeptidases	Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.	Carboxypeptidase
D006020	Glycopeptides	Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.	Glycopeptide
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
D001216	Asparagine	A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)	L-Asparagine
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin
D014644	Genetic Variation	Genotypic differences observed among individuals in a population.	Genetic Diversity,Variation, Genetic,Diversity, Genetic,Diversities, Genetic,Genetic Diversities,Genetic Variations,Variations, Genetic