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At least 19 recordsLinked to original sources
PubMed1962

Zinc in bone.

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Bone and Bones↗
PubMed1962

Hydrolysis of adenosine triphosphate by crystalline yeast pyrophosphatase. Effect of zinc and magnesium ions.

Schlesinger and Coon's report that crystalline yeast inorganic pyrophosphatase, in addition to its known ability to hydrolyze inorganic pyrophosphate in the presence of Mg ions, is also able to catalyze the hydrolysis of ATP and ADP in the presence of Zn ions was confirmed. A systematic study showed that the ratio of 370 of PPase-Mg over ATPase-Zn activities per milligram protein in various preparations of pyrophosphatase obtained in the course of isolation of crystalline pyrophosphatase from baker's yeast was nearly identical in all the preparations, independent of their purity. The course of hydrolysis of ATP by crystalline pyrophosphatase in the presence of Zn was carried out with the aid of ion exchange on Dowex 1. The finding of Schlesinger and Coon that the hydrolysis proceeds from ATP to ADP and then slowly to AMP was confirmed. The kinetics of the first phase of the reaction was found to depend on the molar ratio of Zn/ATP in the reaction mixture. Mg ions in the presence of Zn ions have an accelerating effect on the rate of hydrolysis of ATP. This suggests strongly that both activities-ATPase and PPase-are manifestations of the same active group in the protein molecule of crystalline pyrophosphatase.

Adenine Nucleotides↗
PubMed1962

Isolation of a protective gamma-globulin fraction interfering with the zinc sulphate turbidity test.

The serum of a case of hyperglobulinaemia with negative thymol and zinc sulphate turbidity reactions was studied. The serum when added to pathological sera with high turbidity values brought about a marked reduction in the original turbidity values. Also, the serum did not give the usual copper proteinate precipitate when added to copper sulphate solutions. The anomalous protein fraction responsible for the above properties was isolated from the gamma globulins by precipitation at 28% saturation with ammonium sulphate. It was found to be neither a macroglobulin (Waldenstrom's), a cryoglobulin, nor a collagen protein. Its occurrence in the very gamma globulin fraction which is responsible for many of the turbidity reactions is of great significance in the interpretation of these tests. It is suggested that the normal turbidity and flocculation reactions reported in some cases of multiple myelomatosis might be due to some such anomalous proteins.

Copper↗