title: Amino acid sequence of derivatives of newborn rat epidermal thiol proteinase inhibitor.
abstract: Three different forms of thiol proteinase inhibitor (TPI) were isolated from newborn rat epidermis, in which two forms, TPI-1 and TPI-2, inhibited a proteinase activity, but another newly detected one (designated as TPI-3), showed no inhibitory effect. The complete amino acid sequence of TPI-2 and the sequence of the first seventeen residues from the NH2-terminus of TPI-3 were determined. The sequence shows that TPI-2 lacks in the first six (or four) residues from the NH2-terminus of intact inhibitor, TPI-1, whereas TPI-3 is devoid of its fifteen amino acid residues. These results indicate a high and specific susceptibility of TPI to proteolysis. Most significantly, the NH2-terminal region of TPI appears to be essential for inhibition of proteinase activity.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000831:Animals, Newborn; D003488:Cyanogen Bromide; D004589:Electrophoresis, Disc; D006868:Hydrolysis; D010455:Peptides / Q000032:analysis; D011480:Protease Inhibitors / Q000032:analysis*; D051381:Rats
chemical_list: D000596:Amino Acids; D010455:Peptides; D011480:Protease Inhibitors; D003488:Cyanogen Bromide