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S A Adams

Publications and source records attributed to S A Adams.

24 records · Page 2Linked to original sources
PubMed1989

Brain natriuretic peptides: differential localization of a new family of neuropeptides.

Brain natriuretic peptide (BNP) is a recently discovered neuropeptide, isolated from the porcine brain, that is highly homologous to atriopeptin (AP), the atrial natriuretic peptide. We used a set of highly selective antisera against the two peptides to map their differential distribution immunohistochemically in the rat central nervous system. BNP immunoreactivity has a distinct distribution, involving many central autonomic and endocrine control structures that contain little if any AP immunoreactivity. AP and BNP belong to a family of neuropeptides that may be important in central cardiovascular control.

Animals↗
PubMed1981

Purification and properties of a gelatin-specific neutral protease from human skin.

A neutral protease with a marked specificity for gelatin as a protein substrate has been purified to homogeneity from medium of human skin in serum-free explant culture. The pH optimum of this gelatinase is between 7.0 and 7.5 with little or no activity displayed below pH 5. Inhibition by EDTA, ethylene glycol bis(beta-amino-ethyl ether)N,N,N',N'-tetraacetic acid (EGTA), and 1,10-phenanthroline suggest that the enzyme is a metalloendopeptidase. Calcium concentration-dependent inhibition of the enzyme by EGTA and EDTA suggest further that there is a requirement for extrinsic calcium. Indeed, removal of calcium and reduces enzyme activity, and subsequent addition of calcium restores full activity. The gelatinase is not inhibited by serine protease inhibitors but is inhibited by cysteine, dithiothreitol, and beta-mercaptoethanol. It is also inhibited by a macromolecular inhibitor of collagenase which has been purified from human skin fibroblasts. The apparent molecular weight of this enzyme, as determined by gel filtration is 120,000-150,000. The enzyme is a glycoprotein, as indicated by staining with periodic acid-Schiff reagent and by its affinity for lectins. Human skin gelatinase shows little or no reactivity toward common protein substrates, such as hemoglobin or casein, and does not cleave helical collagen. Two sites of cleavage in the sequence of gelatin, Gly-Ile and Gly-Leu, have been positively identified using synthetic substrates and tryptic peptides of collagen.

Amino Acid Sequence↗