Metabolism of insulin and glucagon. Glutathione-insulin transhydrogenase from microsomes of rat liver.
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Animals↗
Biomedical subjects
H Hanson
Publications and source records attributed to H Hanson.
[Enzyme activity of human milk in relation to amino acid arylamides].
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Acyltransferases↗
[Partial purification and properties of glycyl-L-leucine hydrolase (EC 3.4.3.2) from human milk].
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Cations, Divalent↗
[Studies of the influence of pre-incubation conditions on the enzyme activity of leucine aminopeptidase].
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Buffers↗
Bovine lens leucine aminopeptidase pH dependence of the kinetic parameters.
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Animals↗
Method of visualization of matrix-bound proteins. Leucine aminopeptidase bound to Sepharose and Sephadex beads.
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Animals↗
[Dimerization of leucine aminopeptidase].
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Animals↗
The influence of anions on enzymic activity and metal cation binding of leucine aminopeptidase.
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Acetates↗
Metabolism of insulin and glucagon. Breakdown of radioiodinated insulin and glucagon in rat liver cell fractions.
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Cell Nucleus↗
[Proteolytic activity of psoriacic scales].
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Chromatography, Paper↗
[Does leucine amino-peptidase (3.4.1.1) crystallized from cattle crystalline lenses contain neuraminic acid and alkaline phosphatase activity?].
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Alkaline Phosphatase↗
Intracellular protein breakdown. I. Activity determinations of endoipeptidases using protein substrates.
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Blood Proteins↗
Intracellular protein breakdown. II. Breakdown of proteins from rat liver cytosol by endopeptidase.
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Animals↗
[Glycl-D-leucine- and L-leucineamide-splitting enzyme activities on Sephadex G 200 of crude homogenates of human and rat kidneys].
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Alanine↗
[Intracellular protein breakdown. 3. Intracellular distribution of proteolytic degradation of cytosol proteins at neutral pH].
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Animals↗
[(Leucine) aminopeptidase from Micrococcus lysodeikticus: purification and various properties].
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Chromatography, Gel↗
Zur Bedeutung des Zinks in der Leucinaminopeptidase aus Rinderaugenlinsen.
Leucine aminopeptidase of bovine lens is a zinc metallo-enzyme. A zinc content of 5.0 - 7.6 g-atoms of Zn/M.W. 3.2 x 10(6) was estimated by labelling with 65Zn and by atomic absorption spectrophotometry. By continuous dialysis against o-phenanthroline zinc was almost completely removed. The enzymatically inactive "apo"-enzyme could not be reactivated by addition of Zn(2+). The binding of cadmium, manganeous and cobaltous ions was investigated. With some probability manganese is bound at an other site than zinc. The effect of pH and buffer ions on the binding of zinc to leucine aminopeptidase was demonstrated.
Journal Article↗