Abstract
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 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.
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Abbreviations
- DFP:
-
diisopropylfluorophosphate
- PMSF:
-
phenylmethylsulfonylfluoride
- Glp:
-
pyroglutamyl
- NHC6H4NO2 :
-
p-nitroanilide
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This work was supported in part by a grant from the Russian Foundation for Basic Research.
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Rudenskaya, G.N., Bogdanova, E.A., Revina, L.P. et al. Macluralisin — a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid.. Planta 196, 174–179 (1995). https://doi.org/10.1007/BF00193231
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DOI: https://doi.org/10.1007/BF00193231