Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid

A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 5...

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Veröffentlicht in:	Planta 1995, Vol.196 (1), p.174-179
Hauptverfasser:	Rudenskaya, G.N, Bogdanova, E.A, Revina, L.P, Golovkin, B.N, Stepanov, V.M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence amino acid sequences Amino acids Bacitracin Biotechnology characterization chemical composition Chromatography, Affinity Chromatography, Gel enzyme activity enzyme inhibitors Enzymes Fruit - enzymology fruits glycoproteins Glycoproteins - chemistry Insulin isolation Maclura pomifera Molecular Sequence Data n-terminal sequence phylogeny Plant biochemistry Plant Proteins - chemistry Plant Proteins - isolation & purification Plants Plants - enzymology Sequence Homology, Amino Acid Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification serine proteinases Sorbents Soybeans Substrate Specificity substrates subtilisin Subtilisins - chemistry Subtilisins - isolation & purification temperature Trypsin inhibitors Ungulates
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