scholarly journals Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity

1976 ◽  
Vol 155 (1) ◽  
pp. 127-135 ◽  
Author(s):  
A K Allen ◽  
N N Desai ◽  
A Neuberger
Keyword(s):  
Affinity Chromatography ◽  
Vicia Faba ◽  
Acid Derivative ◽  
Concanavalin A ◽  
Broad Bean ◽  
Soya Bean ◽  
Hexanoic Acid ◽  
The Other ◽  
Amino Group ◽  
Strong Inhibition

1. The lectin from the broad bean (Vicia faba) was purified by affinity chromatography by using 3-O-methylglucosamine covalently attached through the amino group to CH-Sepharose (an omega-hexanoic acid derivative of agarose). Its composition and the nature of its subunits were compared with concanavalin A and the lectins from pea and lentil. 2. Unlike the other three lectins, broad-bean lectin is a glycoprotein; a glycopeptide containing glucosamine and mannose was isolated from a proteolytic digest. 3. The mol.wt. is about 47500; the glycoprotein consists of two apprently identical subunits, held together by non-covalent forces. Fragments of the subunits, similar to those found in concanavalin A and soya-bean agglutinin, were found in active preparations. 4. Broad-bean lectin was compared with concanavalin A and the lectins from pea and lentil in an investigation of the inhibition of their action by a number of monosaccharides, methyl ethers of monosaccharides, disaccharides and glycopeptides. The most striking differences concern 3-O-substituted monosaccharides, which are strong inhibitors of the action of broad-bean, pea and lentil lectins but not of the action of concanavalin A. There is, however, no strong inhibition of the action of these lectins by 3-Olinked disaccharides.

scholarly journals Development and transfer character of secretory glands in the broad bean (Vicia faba L.)

2014 ◽  
Vol 50 (3) ◽  
pp. 391-398 ◽  
Author(s):  
Jadwiga A. Tarkowska ◽  
Alicja M. Zobel ◽  
Małgorzata Maciak
Keyword(s):  
Cell Wall ◽  
Vicia Faba ◽  
Shoot Apex ◽  
Broad Bean ◽  
The Other ◽  
Size And Shape ◽  
Gland Cells ◽  
Vicia Faba L ◽  
Secretory Glands ◽  
Intensive Development

The development and transfer character of the secretory glands developing ,on the stipules (from node I to X) in <em>Vicia faba</em> L. was investigated. It was found that the state of developmental and functional maturity is reached by them in nodes IV-VI from the shoot apex. In mature glands the characteristic ingrowths from the cell wall to the interior of the protoplast develop to different extents (number, size and shape) in the particular gland cells. Their most intensive development up to the formation of labyrinths was observed in the outher walls of the head, and particularly in the cells of its upper tier. In all the other cells of the gland (up to the subepidermal one) less developed ingrowths occur on the transverse walls and even less along the long axis of the gland. This arrangement of the ingrowths shows the direction of flow of secretive substances.

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

Activation of latent collagenase from polymorphonuclear leukocytes by cathepsin G

1979 ◽  
Vol 44 (10) ◽  
pp. 3177-3182 ◽  
Author(s):  
Mária Stančíková ◽  
Karel Trnavský
Keyword(s):  
Affinity Chromatography ◽  
Trypsin Inhibitor ◽  
Polymorphonuclear Leukocytes ◽  
Soya Bean ◽  
Cathepsin G ◽  
Sepharose Column ◽  
Bean Trypsin Inhibitor ◽  
Human Polymorphonuclear Leukocytes

Cathepsin G was isolated from human polymorphonuclear leukocytes and purified by affinity chromatography on Antilysin-Sepharose column. Purified enzyme activated later collagenase isolated from leukocytes. Activation at 36°C was maximal after 30 min incubation. Inhibitors of cathepsin G - soya-bean trypsin inhibitor, diisopropyl phosphofluoridate and Antilysin were active in inhibiting the activation of latent collagenase by cathepsin G.

scholarly journals Raw soya-bean flour increases cholecystokinin release in man

1987 ◽  
Vol 58 (2) ◽  
pp. 175-179 ◽  
Author(s):  
John Calam ◽  
Joanna C. Bojarski ◽  
Caroline J. Springer
Keyword(s):  
Heat Treatment ◽  
Trypsin Inhibitor ◽  
Soya Bean ◽  
The Other ◽  
Oral Ingestion ◽  
Pancreatic Acini ◽  
Bean Flour ◽  
Heat Treated ◽  
Releasing Effect ◽  
Cck Release

1. The aim of the present study was to determine whether oral ingestion of raw soya-bean flour, which contains trypsin inhibitors, alters the release of cholecystokinin (CCK) in man.2. Eleven healthy volunteers ate two mixed meals: one with raw soya-bean flour and the other with soya-bean flour that had been heat-treated. The two flours inhibited 34 and 3 mg trypsin/g flour respectively.3. CCK was measured in plasma using a bioassay based on the release of amylase (EC 3.2.1.1) from dispersed rat pancreatic acini.4. The peak CCK response was 168 (SE 8.1) pmol/l with raw soya-bean flour but 4.9 (SE 2.8) pmol/l with heat-treated flour (P < 0.05).5. We conclude that ingestion of raw soya-bean flour increases CCK release in man and that heat treatment which reduces the trypsin inhibitor content of the flour also diminishes its CCK-releasing effect.

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