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Subtilisin inhibitors in legume seeds.

Seidl, D. S. ; Lorenzo, P. LU ; Pinelli, B. E. and Tovar, J. LU orcid (1988) In Biological Chemistry Hoppe-Seyler 369 Suppl. p.69-73
Abstract

Subtilisin inhibitors (SI) having an average molecular mass of 8 kDa purified from jack beans (Canavalia ensiformis) and broad beans (Vicia faba) to electrophoretical homogeneity are compared to those isolated from chick peas (Cicer arietinum) and black beans (Phaseolus vulgaris). The specificity spectrum of SI is restricted to microbial serine proteinases. Their interaction with subtilisin Carlsberg is variable, obtaining the highest value for black bean, followed by broad bean, chick pea and jack bean inhibitors. Proteinase K reacts with most SI twice as strongly as subtilisin. The reaction of SI with subtilisin apparently follows the "standard mechanism" proposed by Laskowski for the interaction of trypsin with its inhibitors.... (More)

Subtilisin inhibitors (SI) having an average molecular mass of 8 kDa purified from jack beans (Canavalia ensiformis) and broad beans (Vicia faba) to electrophoretical homogeneity are compared to those isolated from chick peas (Cicer arietinum) and black beans (Phaseolus vulgaris). The specificity spectrum of SI is restricted to microbial serine proteinases. Their interaction with subtilisin Carlsberg is variable, obtaining the highest value for black bean, followed by broad bean, chick pea and jack bean inhibitors. Proteinase K reacts with most SI twice as strongly as subtilisin. The reaction of SI with subtilisin apparently follows the "standard mechanism" proposed by Laskowski for the interaction of trypsin with its inhibitors. Accordingly, the reactive site of jack bean, broad bean and black bean SI is reversibly cleaved by subtilisin in acid and neutral solutions, whereas chick pea SI is hydrolysed only at neutral pH values. Judged by similarities in specificity, molecular mass, heat stability and reactive site cleavage, the SI from legume seeds could constitute a new "family" of proteinase inhibitors.

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author
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publishing date
type
Contribution to journal
publication status
published
subject
in
Biological Chemistry Hoppe-Seyler
volume
369 Suppl
pages
5 pages
publisher
De Gruyter
external identifiers
  • pmid:3060146
  • scopus:0024015071
ISSN
0177-3593
language
English
LU publication?
no
id
3a8b43d3-4641-4fca-a920-c660ed34d823
date added to LUP
2018-10-05 16:45:40
date last changed
2024-01-15 02:55:20
@article{3a8b43d3-4641-4fca-a920-c660ed34d823,
  abstract     = {{<p>Subtilisin inhibitors (SI) having an average molecular mass of 8 kDa purified from jack beans (Canavalia ensiformis) and broad beans (Vicia faba) to electrophoretical homogeneity are compared to those isolated from chick peas (Cicer arietinum) and black beans (Phaseolus vulgaris). The specificity spectrum of SI is restricted to microbial serine proteinases. Their interaction with subtilisin Carlsberg is variable, obtaining the highest value for black bean, followed by broad bean, chick pea and jack bean inhibitors. Proteinase K reacts with most SI twice as strongly as subtilisin. The reaction of SI with subtilisin apparently follows the "standard mechanism" proposed by Laskowski for the interaction of trypsin with its inhibitors. Accordingly, the reactive site of jack bean, broad bean and black bean SI is reversibly cleaved by subtilisin in acid and neutral solutions, whereas chick pea SI is hydrolysed only at neutral pH values. Judged by similarities in specificity, molecular mass, heat stability and reactive site cleavage, the SI from legume seeds could constitute a new "family" of proteinase inhibitors.</p>}},
  author       = {{Seidl, D. S. and Lorenzo, P. and Pinelli, B. E. and Tovar, J.}},
  issn         = {{0177-3593}},
  language     = {{eng}},
  month        = {{05}},
  pages        = {{69--73}},
  publisher    = {{De Gruyter}},
  series       = {{Biological Chemistry Hoppe-Seyler}},
  title        = {{Subtilisin inhibitors in legume seeds.}},
  volume       = {{369 Suppl}},
  year         = {{1988}},
}