A new esteroproteinase (proteinase F) from the submandibular glands of female mice

Biochim Biophys Acta. 1983 Mar 31;756(2):163-70. doi: 10.1016/0304-4165(83)90088-0.

Abstract

One of the esteroproteinases present in the submandibular glands of female mice was purified and characterized. The enzyme, designated proteinase F in this report, had a pI value of 4.6 and a molecular weight of 27600, being comprised of two subunits of 10000 and 18000 daltons. The amino acid composition of proteinase F resembled that of the epidermal growth factor-binding protein, but antiserum against proteinase F only reacted weakly against the binding protein. Proteinase F had an optimum pH at around 9.0 and was strongly inhibited by Cu2+ and Hg2+ (42 and 76% inhibition, respectively, at a concentration of 4 x 10(-6) M). It was also inhibited by aprotinin, phenylmethylsulfonylfluoride, iodoacetamide, leupeptin, antipain, and benzamidine but neither by trypsin inhibitors from pancrease, soybean, or ovomucoid, nor by TLCK, TPCK, and epsilon-amino-n-caproic acid. Although its actual physiological function has yet to be determined, these properties indicate that proteinase F is a new enzyme, being distinguished from known proteinases, kallikrein, plasmin, trypsin, chymotrypsin, tonin, angiotensin-converting enzyme, proteinase A (beta-nerve growth factor endopeptidase), proteinase D (epidermal growth factor-binding protein), P-esterase, renin A, and renin C. Proteinase F was present in the submandibular glands of female mice more abundantly than in those of males, but it increased in males following castration. Thus, proteinase F appears to be affected by male hormones in vivo.

MeSH terms

  • Amino Acids / isolation & purification
  • Animals
  • Castration
  • Chemical Phenomena
  • Chemistry
  • Endopeptidases / isolation & purification*
  • Endopeptidases / metabolism
  • Female
  • Male
  • Mice
  • Mice, Inbred ICR
  • Protease Inhibitors / pharmacology
  • Serine Endopeptidases*
  • Sex Factors
  • Submandibular Gland / enzymology*

Substances

  • Amino Acids
  • Protease Inhibitors
  • Endopeptidases
  • Serine Endopeptidases
  • proteinase F