A procedure is described for isolating the enzyme ribonuclease T(1) from Takadiastase, an extract of the mould Aspergillus oryzae. It involves an initial concentration of the enzyme by adsorption on DEAE-cellulose followed by gradient elution. Later the enzyme is chromatographed on the same adsorbent with an eluent of constant composition. Yields of 350-380mg of ribonuclease T(1) from 500g of Takadiastase were obtained.

Amylases↗

PubMed1970

Measurement of graft-versus-host reactions on the chorioallantoic membrane of the chicken.

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Animals↗

PubMed1969

Stimulation of graft versus host splenomegaly by thymectomy of the donor.

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Animals↗

PubMed1967

Effect of neuraminidase on isozymes of alkaline phosphatase and leucine aminopeptidase.

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Alkaline Phosphatase↗

PubMed1967

Alkaline phosphatase and leucine aminopeptidase association in plasma of the chicken.

Two electrophoretic vari ants of leucine aminopeptidase show direct association with two genetically controlled forms of alkaline phosphatase. Treatment of plasma with neuraminidase converted the faster-migrating form of both enzymes to slower-moving forms, but plasmas with slowermigrating forms were unaffected by this treatment. The two forms of the enzymes may be due to the presence or absence of a single gene controlling the attachment of sialic acid to the enzyme molecules.

Alkaline Phosphatase↗

PubMed1965

Inheritance of two alkaline phosphatase variants in fowl plasma.

Starch-gel electrophoresis of plasina reveals two mnutually exclusive forms of alkaline phosphatase. Analysis of the plasma of 931 birds from 96 sib families of two inbred lines through two generations shows that the faster-moving isozymne is determined by an autosomal gene Ap(2) which is completely dominant to its allele Ap(4) determining the slower form.

Alkaline Phosphatase↗