Purification of galactose-binding phytoagglutinins and phytotoxin by affinity column chromatography using sepharose

Zusammenfassung Phytoagglutinine, welche Galaktose spezifisch binden, wurden mit Chromatographie an Sepharose gereinigt. Zwei Fraktionen ausRicinus communis-Agglitomom wiurden durch Gelfiltration mittels Bio-gel getrennt: die früh eluierte Fraktion zeigte starke Agglutinationsaktivität und schwache Toxizität, während die später eluierte Fraktion eine schwache Agglutinatinsaktivität bei starker Toxizität zeigt.

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We thank Dr. Y.Sakurai, Department of Chemotherapy, Cancer Istitute, for his constant interest and encouragement during the execution of this work.     

Purification of 2-deoxy-2-dansylamido-D-glucose by affinity chromatography on a lectin-loaded agarose column

Summary A method is demonstrated to purify 2-substituted derivatives of glucose and sterically related sugars by affinity chromatography on Con A-sepharose. The method seems to be of rather general applicability.     

Purification of 2-deoxy-2-dansylamido-D-glucose by affinity chromatography on a lectin-loaded agarose column.

A method is demonstrated to purify 2-substituted derivatives of glucose and sterically related sugars by affinity chromatography on Con A-sepharose. The method seems to be of rather general applicability.     

The lectin fromViscum album L. purification by biospecific affinity chromatography

Summary A lectin fromViscum album which specifically binds to D-galactose was isolated by affinity chromatography on O-lactosyl-, O-galactosyl-polycarylamide or hydrolized sepharose 4 B. Some serological and physicochemical properties of the agglutinin are reported.     

Evidence of soluble proteins binding adriamycin by affinity chromatography

Summary The presence in various tissues of soluble proteins binding adriamycin is evidenced by affinity chromatography.     

Evidence of soluble proteins binding adriamycin by affinity chromatography.

The presence of various tissues of soluble proteins binding adriamycin is evidenced by affinity chromatography.     

Rat liver S-adenosyl-L-homocysteine hydrolase purification by affinity column chromatography (author's transl)]

S-adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) has been purified 240-fold from rat liver by affinity column chromatography on aminohexyl sepharose bound 6-mercaptopurine 9 D-riboside. The purified enzyme was homogeneous by gel electrophoresis.     

Purification of mouse liver thymidylate synthetase by affinity chromatography using 10-methyl-5,8-dideazafolate as the affinant

Summary Thymidylate synthetase (methylenetetrahydrofolate: 2-deoxyuridine-5-monophosphate C-methyltransferase; EC 2.1.1.45) from neonatal mouse liver has been purified 714-fold by affinity chromatography on aminohexylsepharose bound 10-methyl-5,8-dideazafolate.Supported by grant CA22754, awarded by the National Cancer Institute, DHEW.     

Separation of specific fractions of synaptosomes by affinity chromatography

Summary The authors describe a new technique for isolation of specific fractions of synaptosomes, on the basis of their surface glycoproteins, by affinity chromatography using lectin-Sepharose columns.     

Isolation of Myxovirus influenzae surface antigens by affinity chromatography]

Surface antigens of Myxovirus influenzas A/r8/34 and A/Hong Kong/1/68 were isolated on Fetuin covalently attached to Sepharose. The amino acid composition of isolated neuraminidases was determined.