Substitution of Milk for Serum in the Production of Human Leukocyte Interferon

The presence of serum in suspensions of Sendai-induced human leukocytes is necessary for the synthesis of significant amounts of interferon. Very little interferon is obtained from serum-free suspensions. Cow's milk or milk casein can substitute for serum in the production of high yields of human leukocyte interferon.     

Isolation of Inhibitory Factor in Raw Milk Whey Active Against Propionibacteria

Preparative isolation of the active component(s) in skim milk whey inhibitory for propionibacteria was made by using (NH(4))(2)SO(4) salt fractionation. The crude preparation was further purified by Sephadex G-100 column separation. Disc-gel electrophoresis of the active peak from the Sephadex elution pattern (peak I) showed that this fraction contained almost all of the immune globulin in the column sample. The biologically inactive peaks did not contain any immune globulin. Starch-gel electrophoresis of the active peak revealed the presence of three separate immune globulin fractions. A correlation was also observed between hemolytic reaction of propionibacterial strains and relative resistance to whey inhibition. The investigation showed that one of the immune globulins of milk, pseudoglobulin, was mainly responsible for the suppressive activity of whey.     

Fate of Carbon Passing Through the Glucose Pool of Rumen Digesta

The metabolism of the free glucose pool in rumen digesta from sheep fed roughage rations was studied by adding an insignificant quantity of glucose as uniformly labeled (14)C-glucose of high specific activity to in vitro incubation systems. In all experiments wherein only trace quantities of glucose were added to digesta, most of the (14)C-glucose entered acetate. This was true whether label was presented either as a single dose or by continuous addition over a period of 2 hr. Digesta collected at all times after feeding either once daily or at hourly intervals gave similar glucose dissimilation patterns. If, however, a relatively large quantity of carrier glucose was added together with the tracer, the (14)C-acetate: (14)C-propionate ratio was reduced by a factor of about 10. Physical removal of most of the protozoa from digesta generally had little effect on the dissimilation of (14)C-glucose added in tracer amounts, but in one experiment there was a decreased turnover of the free glucose pool and a marked reduction in (14)C entering butyrate. The paucity of (14)C entering propionate when only trace amounts of glucose were added to digesta suggests that this acid was largely formed from substrates whose carbon did not equilibrate with that in free glucose or with that in intermediates of free glucose metabolism.     

Degradation of Linuron and Some Other Herbicides and Fungicides by a Linuron-Inducible Enzyme Obtained from Bacillus sphaericus

Linuron [3-(3,4-dichlorophenyl)-1-methoxy-1-methylurea] induces the formation of an enzyme (acylamidase) responsible for the degradation of a large variety of different herbicides and fungicides of the acylanilide and phenylurea type. The former type is degraded at a rate at least 10 times higher than the latter.     

Infectivity and Sedimentation of Rhinovirus Ribonucleic Acid

Ribonucleic acid extracted from the virions of two human rhinoviruses is infective and is similar in size to poliovirus ribonucleic acid.     

Reconstitution of Bacterial Spore Coat Layers In Vitro

The spore coat layers of Bacillus cereus T can be at least partially restored by mixing spores stripped of their coat with solubilized coat protein.     

Ribonucleic Acid Synthesis in Bacteria Treated with Toluene

Escherichia coli and Bacillus megaterium rendered permeable to ribonucleoside triphosphates by toluene treatment retain the capacity to synthesize discrete ribonucleic acid species.     

Complementary Functioning of Nitrogenase Components from a Blue-Green Alga and a Photosynthetic Bacterium

Nitrogenases from Anabaena cylindrica and Chloropseudomonas ethylicum were partially purified into two components. A. cylindrica fraction I protein complemented fraction II protein from C. ethylicum. However, the reciprocal cross between C. ethylicum fraction I and A. cylindrica fraction II was negative.