Decreased expression of J11d antigen during monocytic differentiation of M1 myeloid leukemic cells.

Four myeloid cell lines (M1, WEHI-3B D+, FDC-P1, and 32D) were screened for the presence of J11d antigen. One of these cell lines, the myeloid leukemia M1, was found to express a high level of J11d antigen on the cell surface. Recombinant mouse leukemic inhibitory factor (rm-LIF), recombinant human LIF (rh-LIF), and steroids (hydrocortisone and dexamethasone) could induce M1 cells to undergo monocytic differentiation. The level of J11d antigen was greatly reduced after treatment of the cells with LIF or steroids. Western blotting revealed that the apparent molecular weight of the J11d antigen on M1 cells was 45-48 kDa. Furthermore, the level of J11d mRNA was also reduced during LIF-induced differentiation of M1 cells.     

Population increases of buffalo and wildebeest in the Serengeti*

Censuses of buffalo and wildebeest in the Serengeti-Mara region have been carried out by various workers at intervals since 1958. The methods of these censuses, which normally employ a total count, are described and the errors inherent in such techniques are analysed in detail. After the appropriate corrections had been made the results showed that both populations have increased considerably over the years 1961–1971.     

Effect of sublethal concentrationsof mercury, cadmium, and copper salts on the lysozyme content in fryof the lena river sturgeon acipenser baeri

The paper presents data on a change in lysozyme content in tissues of spleen, liver and heart in fry of the Lena River sturgeon exposed to the presence of sublethal concentrations of Hg2⁺, Cd²⁺, and Cu²⁺ under conditions of chronic experiment. It has been shown that the lysozyme content in fish tissues varies and has a phasic character. The amplitude of fluctuations of this parameter depends on the moment of sampling, nature of the toxicant, and structural-functional organization of the studied organs.     

Syntheses of (Z)-and (E)-4-amino-2-(trifluoromethyl)-2-butenoic acid and their inactivation of gamma-aminobutyric acid aminotransferase.

(Z)- and (E)-4-amino-2-(trifluoromethyl)-2-butenoic acid (4 and 5, respectively) were synthesized and investigated as potential mechanism-based inactivators of gamma-aminobutyric acid aminotransferase (GABA-AT) in a continuing effort to map the active site of this enzyme. The core alpha-trifluoromethyl-alpha,beta-unsaturated ester moiety was prepared via a Reformatsky/reductive elimination coupling of the key intermediates tert-butyl 2,2-dichloro-3,3,3-trifluoropropionate and N,N-bis(tert-butoxy-carbonyl)glycinal. Both 4 and 5 inhibited GABA-AT in a time-dependent manner, but displayed non-pseudo-first-order inactivation kinetics; initially, the inactivation rate increased with time. Further investigation demonstrated that the actual inactivator is generated enzymatically from 4 or 5. This inactivating species is released from the active site prior to inactivation, and as a result, 4 and 5 cannot be defined as mechanism-based inactivators. Furthermore, 4 and 5 are alternate substrates for GABA-AT, transaminated by the enzyme with Km values of 0.74 and 20.5 mM, respectively. Transamination occurs approximately 276 and 305 times per inactivation event for 4 and 5, respectively. The enzyme also catalyzes the elimination of the fluoride ion from 4 and 5. A mechanism to account for these observations is proposed.