Isolation of two endo-beta-N-acetylglucosaminidases from fig latex

Biochim Biophys Acta. 1981 Aug 13;660(2):278-83. doi: 10.1016/0005-2744(81)90171-6.

Abstract

Two endo-beta-N-acetylglucosaminidases (mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase, EC 3.2.1.96) (type F-I and type F-II) have been isolated from fig latex. At pH 7.0, type F-1 was retained by the DEAE-Sephadex A-50 column, whereas type F-II was not adsorbed by the column. The optimum pH of type F-I was found to be pH 5.9 and type F-II, pH 5.4. Type F-I enzyme hydrolyzes the tri-mannosyl derivatives di-N-acetylglucosaminylasparagine faster than the penta- or hexa-mannosyl compounds. Type F-II hydrolyzes the penta- and hexa-mannosyl derivatives, but not the tri-mannosyl compound.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylglucosaminidase / isolation & purification
  • Acetylglucosaminidase / metabolism*
  • Drug Stability
  • Glycopeptides / metabolism
  • Hexosaminidases / metabolism*
  • Hydrogen-Ion Concentration
  • Latex / analysis*
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Molecular Weight
  • Plants / enzymology*
  • Substrate Specificity

Substances

  • Glycopeptides
  • Latex
  • Hexosaminidases
  • Acetylglucosaminidase
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase