Properties of aminopeptidases from bean seeds

Blättler, R; Feller, Urs (June 1987). Properties of aminopeptidases from bean seeds. Experientia, 43(6), p. 659. Basel: Birkhäuser Verlag

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Aminopeptidase forms, extracted from ungerminated bean seeds (Phaseolus vulgar& L., var. 'Saxa'), were separated by ion exchange and gel chromatography. The activities were detected with the following L-amino acid-p-nitroanilides: gly, ala, lys, arg, leu, met and phe as substrates. Some properties of four forms differing in their substrate specificities (1: ala/lys/arg; 2: leu/met/phe; 3: gly; 4: phe) were further investigated. The pHoptima were broad and similar for forms 1 and 2 (around pH 7.25), while gly was most rapidly liberated about pH 8.0 and form 4 was most active around pH 7.0. The form liberating ala, lys and arg was highly sensitive to 1,10-phenanthroline, but the same concentration of this chelator had no major effect on the other forms. The activities of forms 2, 3 and 4 decreased after addition of MgC12, while form '1 was more tolerant in this respect. The inactivation of forms 1,2 and 3 was accelerated by the addition of endopeptidases. The form acting on phe was less sensitive to these treatments.

Item Type:

Conference or Workshop Item (Paper)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Plant nutrition [discontinued]
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS)

UniBE Contributor:

Feller, Urs

Subjects:

500 Science > 580 Plants (Botany)

ISSN:

0014-4754

Publisher:

Birkhäuser Verlag

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

13 Jan 2017 09:41

Last Modified:

05 Apr 2017 09:43

Additional Information:

DOI: 10.1007/BF02126358

BORIS DOI:

10.7892/boris.91916

URI:

https://boris.unibe.ch/id/eprint/91916

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