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At least 217 records · Page 12Linked to original sources
PubMed1977

[Inhibitors for trypsin and chymotrypsin in seeds of the broad bean (Vicia faba) (author's transl)].

Several inhibitors for trypsin and chymotrypsin were detected in seeds of Vicia faba by isoelectric focussing. Their isoelectric points are at pH 8.5 (main peak with shoulder), at pH 9.1 (minor peak with shoulder) and in the range of pH 9.1-6.4 (several minor peaks with significant lower activities). From the mixture of inhibitors obtained by affinity chromatography on carrier bound trypsin, three inhibitors were isolated by preparative electrophoresis in polyacrylamide gel. On electrophoresis these inhibitors behaved uniformly at pH 9.2 and at pH 4.0. Their molecular weights are about 6000 daltons. The amount of basic amino acids is high, while methionine and isoleucine are absent. Beside of trypsin and chymotrypsin some serine proteinases of microbiol origin are inhibited. The thermal stability is quite high. The Vicia inhibitors therefore differ significantly from the Phaseolus inhibitors in several properties.

Chymotrypsin↗
PubMed2002

Chemical composition and ultrastructure of broad bean (Vicia faba L.) nodule endodermis in comparison to the root endodermis.

Ultrastructure and development of apoplastic barriers within indeterminate root nodules formed by Vicia faba L. were examined by light and electron microscopy. The nodule outer cortex is separated from the inner cortex by a heavily suberized nodule endodermis, which matures in submeristematic regions and possesses suberin lamellae. Unsuberized passage cells are present near vascular strands, which are surrounded by a vascular endodermis attached on the inner side of the nodule endodermal cell walls. The vascular endodermis appears immediately below the meristematic apex in developmental state I (Casparian bands), gradually develops suberin lamellae, and attains developmental state II at the base of the nodule. For chemical analysis apoplastic barrier tissues were dissected after enzymatic digestion of non-impregnated tissues. Root epidermal and endodermal cell walls as well as nodule outer cortex could be isolated as pure fractions; nodule endodermal cell walls could not be separated from vascular endodermal cell walls and enclosed xylem vessels. Gas chromatography-flame ionization detection and gas chromatography-mass spectrometry were applied for quantitative and qualitative analysis of suberin and lignin in isolated cell walls of these tissues. The suberin content of isolated endodermal cell walls of nodules was approximately twice that of the root endodermal cell walls. The suberin content of the nodule outer cortex and root epidermal cell walls was less than one-tenth of that of the nodule endodermal cell wall. Substantial amounts of lignin could only be found in the nodule endodermal cell wall fraction. Organic solvent extracts of the isolated tissues revealed long-chain aliphatic acids, steroids, and triterpenoid structures of the lupeol type. Surprisingly, extract from the outer cortex consisted of 89% triterpenoids whereas extracts from all other cell wall isolates contained not more than 16% total triterpenoids. The results of ultrastructural and chemical composition are in good correspondence and underline the important role of the examined tissues as apoplastic barriers.

Biopolymers↗
PubMed1994

Isolation of a potassium-selective ion channel from the plasma membrane of the broad bean Vicia faba L.

Potassium ions are essential for plant nutrition and play an important role in osmoregulation and plant movement. Recent patch clamp investigations and molecular analysis have identified voltage-dependent potassium channels responsible for translocation of this ion across plant membranes. In order to characterize these transporters on the biochemical level, a potassium channel protein was isolated from Vicia faba under preservation of its functional integrity. Potassium channel activity was monitored by tracer flux and black lipid bilayer measurements. The capability for K+ transport copurified with a 67 kDa protein from V. faba plasma membranes. A monoclonal antibody directed against the 67 kDa protein blocked channel activity. Single channels with a unit conductance of 40 pS were highly selective for K+ over Na+.

Biological Transport↗