Solubilization of udp-glucose collagen glucosyltransferase activities from chick embryo liver: Golgi apparatus, smooth and rough endoplasmic reticulum
Author:
Publisher
Elsevier BV
Subject
Biochemistry
Reference21 articles.
1. Perturbation of the structure and function of a membranous Ca2+-ATPase by non solubilizing concentrations of a non-ionic detergent;Andersen;Eur. J.Biochem.,1983
2. Stimulation of collagen galactosyltransferase and glucosyltransferase activities by lysophosphatidylcholine;Anttinen;Biochem.J.,1976
3. Tissue fractionation studies.V.The association in acid phosphatase with a special class of cytoplasmic granules in rat liver;Appelmans;Biochem.J.,1955
4. Characterization of collagen hydroxylysyi glucosyltransferases as mainly intramembranous microsomal enzymes;Blumenkrantz;J.biol.Chem.,1984
5. Evidence of partial localization in Golgi apparatus of UDP-glucose collagen glucosyltransferase from chick embryo liver;Bortolato;Int.J.Biochem.,1990
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1. Activity Increase After Extraction of Alkaline Phosphatase from Human Osteoblastic Membranes by Nonionic Detergents: Influence of Age and Sex;Calcified Tissue International;2000-01-01
2. Differential solubilization of osteoblastic alkaline phosphatase from human primary bone cell cultures;The International Journal of Biochemistry & Cell Biology;1996-04
3. Procollagen glucosyltransferase;Enzyme Handbook 12;1996
4. Studies on the mechanism of different collagen glucosyltransferase reactions (golgi apparatus, smooth endoplasmic reticulum, rough endoplasmic reticulum) in chick embryo liver;International Journal of Biochemistry;1992-02
5. Procollagen glucosyltransferase;Springer Handbook of Enzymes
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