Rapid purification of lactate dehydrogenase X from mouse testes by two steps of affinity chromatography on oxamate-sepharose

Summary At concentrations of 200 M NADH and 0.5M NaCl LDH-X is separated from the other LDH isozymes of mouse testes on oxamate-sepharose. In a second step LDH-X is bound to the same matrix at lower NADH and NaCl concentrations and the pure enzyme can subsequently be eluted.Acknowledgment. This work was supported by grants of the Deutsche Forschungsgemeinschaft awarded to the Sonderforschungsbereich 29 Embryonale Differenzierung und Entwicklung.     

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.     

Preparation of a specific ligand for the purification of arylsulfatases by affinity chromatography

Summary The reduction ofp-nitrocatechol sulfate, the artificial substrate of arylsulfatases followed by a condensation of a succinic anhydride, gives a ligand for the purification of the enzyme by affinity chromatography.     

Large-scale purification of hepatitis B surface antigen using affinity chromatography

Summary Large-scale purification of hepatitis B surface antigen, applicable to the preparation of potential vaccines for prevention of hepatitis B, is described. The method involves the following steps: precipitation of serum with polyethylene glycol 6000, affinity chromatography on concanavalin A-Sepharose and on -aminononyl-Sepharose, and isopycnic centrifugation.This study was supported by grant 09011 from the National Heart, Lung and Blood Institute. We thank Dr. B. Hollinger for testing HB_sAg samples by a complement fixation test.     

Improved method of large scale purification of acetylcholinesterase from the electric eel (Electrophorus electricus) by affinity chromatography

Résumé Une méthode basée sur d'affinité chromatographique nous a permis de purifier complètement l'acétylcholinestérase des organes électriques du gymnote (Electrophorus electricus). L'activité spécifique de l'acétylcholinestérase ainsi établie en milligrammes dépasse 950 mM de substrat hydrolysé (acétylcholine)/mg protéine/h et sa pureté a été vérifiée par électrophorèse sur gel de polyacrylamide.

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This work was supported by grants: USPHS No. GM-01839 and U.C. San Francisco Academic Senate Research Committee, Grant No. 46.     

Evidence of soluble proteins binding adriamycin by affinity chromatography.

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

Ontogenesis of lactate dehydrogenase isozyme patterns in two salmonids (Salmo salar andS. trutta)

Zusammenfassung Die ontogenetischen Änderungen des Isoenzym-Musters der Laktatdehydrogenase (LDH) vonSalmo salar undS. trutta wurde mittels Stärkegel-Elektrophorese verfolgt. Während der frühen Entwicklungsstadien (Furchung und Gastrulation) sind allein die «Herz-Banden» vorhanden. In allen geprüften Organen wird die adulte Bandenzahl unmittelbar nach der Dottersack-Resorption erreicht. Im selben Statium weisen Herzmuskel, Auge und Gehirn bereits das adulte Verteilungsmuster auf, während dieses im Skelettmuskel und der Leber erst nach 2–3 Jahren, vor Erreichung der Geschlechtsreife, auftritt.     

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.     

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.     

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.     

Regional distribution of lactate dehydrogenase isoenzymes in adult rat brain.

The highest lactate dehydrogenase (LDH) activity was found in thalamus, statistically significantly less in cerebral and cerebellar cortex and the lowest in pons. LDH1 and LDH4+5 represented 58% and 23% of the total activity in cerebral cortex, 54% and 20% in thalamus, 42% and 4% in cerebellar cortex and 55% and 7% in pons, respectively.     

Influence of serotonin on the radiation sensitivity of lactate dehydrogenase

Zusammenfassung Die Veränderungen in der Strahlenempfindlichkeit von Milchsäuredehydrogenase durch Serotonin, gebraucht als Serotonin-Kreatinin-Sulfat, wurden spektralphotometrisch untersucht. Die Bestrahlungsdosen variierten zwischen 0–9 · 10⁵ R. Die Serotonin-Konzentrationen variierten zwischen 0–1,23 mM. Die D³⁷-Dosis für eine Serotonin-Konzentration von 246M ist ca. 34mal grösser als für die Kontrollen. Der Schutzeffekt kann durch eine Komplexbildung zwischen Serotonin und den Metallionen, die im Enzym-Molekül vorhanden sind, erklärt werden.