scholarly journals Specific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean)

1979 ◽  
Vol 183 (2) ◽  
pp. 381-388 ◽  
Author(s):  
F Serafini-Cessi ◽  
C Franceschi ◽  
S Sperti
Keyword(s):  
Phaseolus Vulgaris ◽  
Affinity Chromatography ◽  
Specific Interaction ◽  
Lymphocyte Transformation ◽  
Kidney Bean ◽  
Step Procedure ◽  
One Step ◽  
Red Kidney Bean ◽  
Antibody Reaction ◽  
Antigen Antibody

Human Tamm-Horsfall glycoprotein inhibits lymphocyte transformation induced by leucoagglutinin and haemagglutinin from Phaseolus vulgaris (red kidney bean). The glycoprotein interacts with the two lectins, giving insoluble precipitates. The interaction with leucoagglutinin is highly specific, and the shape of the precipitin curve is that of an antigen-antibody reaction; precipitation is specifically inhibited by N-acetyl-D-galactosamine. Results are discussed, and it is suggested that inhibition of lymphocyte transformation is due to competition between human Tamm-Horsfall glycoprotein and carbohydrate receptors on lymphocytes for the two lectins. The interaction between human Tamm-Horsfall glycoprotein and Phaseolus vulgaris lectins has been used to develop a one-step procedure for the separation of the two lectins by affinity chromatography on (human Tamm-Horsfall-glycoprotein)-Sepharose.

Comparison of the phytohaemagglutinin from red kidney bean (Phaseolus vulgaris) purified by different affinity chromatography

2008 ◽  
Vol 108 (1) ◽  
pp. 394-401 ◽  
Author(s):  
Jiaoyan Ren ◽  
John Shi ◽  
Yukio Kakuda ◽  
Daniel Kim ◽  
Sophia Jun Xue ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Affinity Chromatography ◽  
Kidney Bean ◽  
Red Kidney Bean

Enteral Crude Red Kidney Bean (Phaseolus vulgaris) Lectin – Phytohemagglutinin – Induces Maturational Changes in the Enterocyte Membrane Proteins of Suckling Rats

Neonatology ◽  
2003 ◽  
Vol 84 (2) ◽  
pp. 152-158 ◽  
Author(s):  
Danuta Kruszewska ◽  
Pawel Kiela ◽  
Åsa Ljungh ◽  
Kennedy H. Erlwanger ◽  
Björn R. Weström ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Membrane Proteins ◽  
Kidney Bean ◽  
Suckling Rats ◽  
Red Kidney Bean

Red kidney bean lectin (phaseolus vulgaris) is a potent CCK releasing stimulus inducing pancreatic growth

1995 ◽  
Vol 108 (4) ◽  
pp. A730 ◽  
Author(s):  
K.H. Herzig ◽  
S. Bardocz ◽  
G. Grant ◽  
R. Nustede ◽  
U.R. Fölsch ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Kidney Bean ◽  
Pancreatic Growth ◽  
Red Kidney Bean

scholarly journals Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and tyrosine

1977 ◽  
Vol 165 (1) ◽  
pp. 121-126 ◽  
Author(s):  
G D Smith ◽  
D V Roberts ◽  
A Daday
Keyword(s):  
Affinity Chromatography ◽  
Competitive Inhibitor ◽  
Chorismate Mutase ◽  
Prephenate Dehydrogenase ◽  
Step Procedure ◽  
One Step ◽  
High Degree ◽  
Sepharose 4B ◽  
Derivatives Of

Several derivatives of phenylalanine and tyrosine were prepared and tested for inhibition of chorismate mutase-prephenate dehydrogenase (EC 1.3.1.12) from Escherichia coli K12 (strain JP 232). The best inhibitors were N-toluene-p-sulphonyl-L-phenylalanine, N-benzenesulphonyl-L-phenylalanine and N-benzloxycarbonyl-L-phenylalanine. Consequently two compounds, N-toluene-sulphonyl-L-p-aminophenylalanine and N-p-aminobenzenesulphonyl-L-phenylalanine, were synthesized for coupling to CNBr-activated Sepharose-4B. The N-toluene-p-sulphonyl-L-p-aminophenylalanine-Sepharose-4B conjugate was shown to bind the enzyme very strongly at pH 7.5. The enzyme was not eluted by various eluents, including 1 M-NaCl, but could be quantitatively recovered by washing with buffer of pH9. Elution was more effective in the presence of 10 mM-1-adamantaneacetic acid, a competitive inhibitor of the enzyme. This affinity-chromatography procedure results in a high degree of purification of the enzyme and can be used to prepare the enzyme in a one-step procedure from the bacterial crude extract. Such a procedure may therefore prove useful in studying this enzyme in a state that closely resembles that in vivo.

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