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Mammalian glycosidases; distribution in the body.

J. Conchie, +2 more
- 01 Feb 1959 - 
- Vol. 71, Iss: 2, pp 318-325
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This article is published in Biochemical Journal.The article was published on 1959-02-01 and is currently open access. It has received 300 citations till now.

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Studies on the Glycosidases of Jack Bean Meal III. CRYSTALLIZATION AND PROPERTIES OF β-N-ACETYLHEXOSAMINIDASE

TL;DR: Studies of pH and thermal inactivation, mixed-substrate analysis, and the Ki values for several competitive inhibitors indicate that the β-N-acetylglucosaminidase and theβ-N -acetylgalactosamidase activities are catalyzed by the same enzyme at the same site.
Journal ArticleDOI

Effect of perorally administered lactobacilli on macrophage activation in mice.

TL;DR: Observations show that L. casei and L. bulgaricus given by p.o. administration are able to activate macrophages in mice and suggest that these bacteria, when passing through the intestinal tract, may be responsible for the enhanced host immune response.
Journal ArticleDOI

Receptor function of mouse sperm surface galactosyltransferase during fertilization

TL;DR: Evidence is presented that mouse sperm binding to the egg zona pellucida is mediated by a sperm galactosyltransferase (GalTase), which recognizes and binds to terminal N-acetylglucosamine (GlcNAc) residues in the zona peelida, which shows clearly that sperm GalTase serves as a principal gamete receptor during fertilization.
Journal ArticleDOI

Studies on the Glycosidases in Jack Bean Meal I. ISOLATION AND PROPERTIES OF α-MANNOSIDASE

TL;DR: One of the two disaccharides synthesized from mannose by α-mannosidase was identified as α-1,6'-linked mannobiose, which is not a polysaccharidase (endoenzyme) in nature.
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