scholarly journals Rapid method for partial purification of rice germ lipase by affinity chromatography.

1979 ◽  
Vol 43 (8) ◽  
pp. 1771-1772 ◽  
Author(s):  
Yoshiki AOYAGI ◽  
Hirotaka YAMASHITA ◽  
Shinji MATSUMOTO ◽  
Tetsujiro OBARA
Keyword(s):  
Affinity Chromatography ◽  
Rapid Method ◽  
Partial Purification

scholarly journals Rapid partial purification of placental glucocerebroside β-glucosidase and its entrapment in liposomes

1977 ◽  
Vol 164 (2) ◽  
pp. 439-445 ◽  
Author(s):  
I P Braidman ◽  
G Gregoriadis
Keyword(s):  
Enzyme Activity ◽  
Organic Solvent ◽  
Affinity Chromatography ◽  
Rapid Method ◽  
Concanavalin A ◽  
Enzyme Preparation ◽  
Partial Purification ◽  
Glucosidase Activity ◽  
Beta Glucosidase

1. A glucocerebroside beta-glucosidase-rich detergent-free preparation was obtained from human placentas by a rapid method combining affinity chromatography on concanavalin A-Sepharose and organic-solvent precipitation. In a typical preparation about 11000 units of the enzyme purified 1500-fold were obtained from five placentas in 2 days. 2. The enzyme preparation also contained other hydrolases, but the extent of their purification was much smaller. 3. Studies on entrapment in liposomes showed that all glucocerebroside beta-glucosidase activity used could be incorporated in neutral egg phosphatidylcholine-cholesterol liposomes. Association with liposomes appeared to discriminate against other proteins, including some of the hydrolases, thus contributing to further purification of the enzyme. More than 95% of the liposome-associated enzyme activity was latent.

Rapid Method for Partial Purification of Rice Germ Lipase by Affinity Chromatography

1979 ◽  
Vol 43 (8) ◽  
pp. 1771-1772
Author(s):  
Yoshiki Aoyagi ◽  
Hirotaka Yamashita ◽  
Shinji Matsumoto ◽  
Tetsujiro Obara
Keyword(s):  
Affinity Chromatography ◽  
Rapid Method ◽  
Partial Purification

scholarly journals A rapid method for the functional reconstitution of amino acid transport systems from rat liver plasma membranes. Partial purification of System A

1988 ◽  
Vol 255 (3) ◽  
pp. 963-969 ◽  
Author(s):  
A R Quesada ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Rapid Method ◽  
Amino Acid Transport ◽  
Plasma Membranes ◽  
Transport Systems ◽  
Partial Purification ◽  
Acid Transport ◽  
Transport Activity ◽  
System A ◽  
System L

A rapid method for the functional reconstruction of amino acid transport from liver plasma-membrane vesicles using the neutral detergent decanoyl-N-glucamide (‘MEGA-10’) is described. The method is a modification of that previously employed in this laboratory for reconstitution of amino acid transport systems from kidney brush-border membranes [Lynch & McGivan (1987) Biochem. J. 244, 503-508]. The transport activities termed ‘System A’, ‘System N’, and ‘System L’ are all reconstituted. The reconstitution procedure is rapid and efficient and is suitable as an assay for transport activity in studies involving membrane fractionation. By using this reconstitution procedure, System A transport activity was partially purified by lectin-affinity chromatography.

A rapid method for the isolation and partial purification of specific eucaryotic messenger RNA's

1972 ◽  
Vol 47 (2) ◽  
pp. 387-392 ◽  
Author(s):  
G.C. Rosenfeld ◽  
J.P. Comstock ◽  
A.R. Means ◽  
B.W. O'Malley
Keyword(s):  
Rapid Method ◽  
Partial Purification

Concentration of Staphylococcal Enterotoxin from Food Extract Using Copper Chelate Sepharose

1989 ◽  
Vol 52 (12) ◽  
pp. 903-905 ◽  
Author(s):  
N. DICKIE ◽  
M. AKHTAR
Keyword(s):  
Rapid Method ◽  
Food Poisoning ◽  
Latex Agglutination ◽  
Staphylococcal Enterotoxin ◽  
Agglutination Test ◽  
Latex Agglutination Test ◽  
Partial Purification ◽  
Copper Chelate ◽  
Food Extract ◽  
Concentration Step

A simple and rapid method is described for detecting as little as 1 ng each of staphylococcal enterotoxins A, B, and C2 in 100 mL samples of food extracts. Samples were fractionated on copper chelate Sepharose 6B and the recovery of added staphylococcal enterotoxin was measured by the reversed passive latex agglutination test. An approximate 100 fold concentration of toxin was obtained. The method should prove useful as a partial purification and concentration step in the analysis of foods incriminated in food poisoning outbreaks.

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