Activity of the respiratory inhibitor RF in human red cells in anaemia

Stroma-free haemolysates of red cells from patients with acute or latent anaemia inhibit the NADH oxidase activity of submitochondrial particles from beef heart. The inhibitory activities appeared significantly more frequently in anaemic patients than in normal persons and are likely due to the action of a factor which is identical or similar to the inhibitory protein RF present in rabbit reticulocytes. The possible use of the inhibitor assay for clinical purpose is under discussion.     

Mouse prolactin obtained by pituitary organ culture in a serum-free medium.

Mouse prolactin was purified by organ culture of pituitaries and electrophoresis of the medium. Mouse pituitaries were organ-cultured in 9-cm Petri dishes containing Waymouth's medium (MB 752/1) supplemented with penicillin (50 units/ml), streptomycin (100mug/ml), and bovine insulin (0.12 I.U./ml) for 8 days. Prolactin-rich culture medium was half-saturated with ammonium sulfate and centrifuged. The pellet was subjected to analytical disc electrophoresis (10% acrylamide). Gels were sectioned into 2-mm segments. Prolactin was eluted in 0.04M phosphate buffer (pH 7.2), dialyzed and lyophylized. Two hundred and forty ml medium in which 360 pituitaries were cultured yielded 29.3 mg lyophylized mouse prolactin. Although the preparation contained 2 other bands on acrylamide gel disc electrophoresis, a single precipitin line was seen in immunodiffusion and immunoelectrophoresis, showing the identity of their antigenicity. From these results, two other proteins in the preparation were suggested to be deamidated prolactin.     

Metabolism of nicotinic acid in plant cell suspension cultures: II; Isolation, characterization and enzymology of nicotinic acid N-alpha-arabinoside (author's transl)]

A very hydrophilic compound was isolated from parsley cell suspension cultures in high yield after application of nicotinic acid. Using chemical, chromatographic and spectroscopic procedures the structure of this new plant constituent has been elucidated as nicotinic acid N-alpha-L-arabinopyranoside. This structure has been proved by chemical synthesis. An arabinosyltransferase was isolated from parsley cell suspension cultures and purified about 19-fold. The enzyme converted nicotinic acid N-alpha-arabinoside with UDP to nicotinic acid and UDP-arabinose. pH-Optimum (pH 7.0-8.0), Km value for nicotinic acid N-alpha-L-arabinoside (2.2 X 10(-4) mol/l) and mol. wt. (app. 70 000) of the transferase were measured. Function and biosynthesis of the arabinoside in cell cultures are discussed.