Biomaterial Database

Functional abnormality of proalbumin Christchurch. 1980

S O Brennan, and R W Carrell

Proalbumin Christchurch is a varient of human albumin in which the C-terminal basic residue of the propeptide has undergone a mutation to glutamine. In this investigation spectral and equilibrium dialysis studies have shown that the variant lacks the high affinity copper binding site of normal albumin. A simple electrophoretic procedure is described using 63Ni(II), which allow discrimination of proalbumins from other variants of albumin. The finding that Proalbumin Christchurch is readily cleaved in vitro by trypsin but is secreted uncleaved in vivo is evidence that propeptide cleavage is due to specific proteolysis with paired basic residues being a pre-requisite.

UI	MeSH Term	Description	Entries
D009532	Nickel	A trace element with the atomic symbol Ni, atomic number 28, and atomic weight 58.69. It is a cofactor of the enzyme UREASE.
D011228	Prealbumin	A tetrameric protein, molecular weight between 50,000 and 70,000, consisting of 4 equal chains, and migrating on electrophoresis in 3 fractions more mobile than serum albumin. Its concentration ranges from 7 to 33 per cent in the serum, but levels decrease in liver disease.	Proalbumin,Transthyretin
D003300	Copper	A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.	Copper-63,Copper 63
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
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012709	Serum Albumin	A major protein in the BLOOD. It is important in maintaining the colloidal osmotic pressure and transporting large organic molecules.	Plasma Albumin,Albumin, Serum
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