In this paper we describe the purification to molecular homogeneity of the enzyme that cleaves the synthetic epidermal mitosis-inhibiting pentapeptide (pyroGlu-Glu-Asp-Ser-Gly; EPP) from swine serum. Biochemical characterisation of the enzyme shows a glycoprotein with apparent molecular mass of 200 kDa. The Km and Kcat values for EPP hydrolysis are 0.624 mM and 694 s-1, respectively. Use of proteinase inhibitors shows the enzyme's metalloendopeptidase character. Moreover, captopril and lisinopril prevent the cleavage of EPP. The N-terminal amino-acid sequence of the purified protein corresponds to the N-terminal amino-acid sequence of swine kidney angiotensin-converting enzyme, a dipeptidyl carboxypeptidase (EC 3.4.15.1).
Purification and characterisation of swine serum proteinase which hydrolyses epidermal inhibitory pentapeptide.
BRAMUCCI, Massimo;MIANO, Antonino;QUASSINTI, Luana;AMICI, Domenico
1996-01-01
Abstract
In this paper we describe the purification to molecular homogeneity of the enzyme that cleaves the synthetic epidermal mitosis-inhibiting pentapeptide (pyroGlu-Glu-Asp-Ser-Gly; EPP) from swine serum. Biochemical characterisation of the enzyme shows a glycoprotein with apparent molecular mass of 200 kDa. The Km and Kcat values for EPP hydrolysis are 0.624 mM and 694 s-1, respectively. Use of proteinase inhibitors shows the enzyme's metalloendopeptidase character. Moreover, captopril and lisinopril prevent the cleavage of EPP. The N-terminal amino-acid sequence of the purified protein corresponds to the N-terminal amino-acid sequence of swine kidney angiotensin-converting enzyme, a dipeptidyl carboxypeptidase (EC 3.4.15.1).I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
