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Featured researches published by A. J. Hay.


Biochimica et Biophysica Acta | 1970

The determination of the individual neutral and amino sugars in carbohydrates.

G. A. Levvy; A. J. Hay; J. Conchie; I. Strachan

Abstract An experimental study has been made of procedures for the acid hydrolysis and methanolysis of sugar polymers. Individual neutral and amino sugars in the products were examined by colorimetric methods and by gas-liquid chromatography of the trimethylsilyl derivatives. Quantitative N -acetylation of amino sugars was carried out with dilute acetic anhydride in aqueous acetone (1:1, v/v) on a column of Dowex 1 (CO 3 2− form). Methanolysis was found to be preferable for the release of neutral sugars from glyco-proteins, whereas acid hydrolysis should be employed for amino sugars.


Biochimica et Biophysica Acta | 1966

The heterogeneity of ovalbumin glycopeptide

G. A. Levvy; J. Conchie; A. J. Hay

Abstract When passed repeatedly down a Sephadex G-25 column, pronase digests of ovalbumin gave glycopeptide fractions with hexose: hexosamine ratios varying progressively from 5:4.8 to 5:2.5. The bulk of the material approximated to a 5:3 ratio, but showed continuous dispersion on recycling on Sephadex. The preparation of pronase contained hexose and yielded a glucose-containing glycopeptide on autodigestion. Errors from this source were avoided by purifying the proteolytic enzyme before use. Pronase was examined for some of the commoner glycosidase activities, with negative results.


Biochemical Journal | 1967

Inhibition of glycosidases by aldonolactones of corresponding configuration: Preparation of (1-->5)-lactones by catalytic oxidation of pyranoses and study of their inhibitory properties.

J. Conchie; A. J. Hay; I. Strachan; G. A. Levvy


Biochemical Journal | 1964

Inhibition of glycosidases by aldonolactones of corresponding configuration. 4. Inhibitors of mannosidase and glucosidase

G. A. Levvy; A. J. Hay; J. Conchie


Biochemical Journal | 1990

Study of the mode of action and site-specificity of the endo-(1→4)-β-d-glucanases of the fungus Penicillium pinophilum with normal, 1-3H-labelled, reduced and chromogenic cello-oligosaccharides

K M Bhat; A. J. Hay; M Claeyssens; Thomas M. Wood


Biochemical Journal | 1961

Mammalian glycosidases. 3. The intracellular localization of β-glucuronidase in different mammalian tissues.

J. Conchie; A. J. Hay; G. A. Levvy


Biochemical Journal | 1959

Mammalian glycosidases. 2. Properties of α-mannosidase and β-galactosidase from rat epididymis

J. Conchie; A. J. Hay


Biochemical Journal | 1957

Properties of limpet β-glucuronidase

G. A. Levvy; A. J. Hay; C. A. Marsh


Biochemical Journal | 1969

The enzymic degradation of ovalbumin and its glycopeptides

J. Conchie; A. J. Hay; I. Strachan; G. A. Levvy


Biochemical Journal | 1970

Purification and properties of α-d-mannosidase from the limpet, Patella vulgata

Sybil M. Snaith; G. A. Levvy; A. J. Hay

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G. A. Levvy

Rowett Research Institute

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J. Conchie

Rowett Research Institute

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I. Strachan

Rowett Research Institute

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K M Bhat

Rowett Research Institute

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Thomas M. Wood

Rowett Research Institute

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C. A. Marsh

Rowett Research Institute

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Sybil M. Snaith

Rowett Research Institute

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