Amino acid sequence of derivatives of newborn rat epidermal thiol proteinase inhibitor.
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.
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
D000596:Amino Acids; D010455:Peptides; D011480:Protease Inhibitors; D003488:Cyanogen Bromide