Disulphide bonds assignment in the inter-alpha-inhibitor heavy chains--structural and functional implications.

Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor. It consists of three polypeptide chains covalently linked by a glycosaminoglycan: a light one named bikunin, carrying the antiproteinase activity and two heavy chains H1 and H2. The amino acid sequences of these heavy chains are highly similar; however when IalphaI is digested by neutrophil proteinases, their proteolytic susceptibility strongly differs [Balduyck, M.

Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine.

The cDNA of a mitochondrial calcium binding protein, "calmitine", has been cloned from a human skeletal muscle cDNA library. One cDNA of 1.8 kb has been isolated and sequenced.