Zobrazeno 1 - 10
of 430
pro vyhledávání: '"O, TOUSTER"'
Autor:
O. WINTERSTEINER, W. R. BOON, H. C. CARRINGTON, D. W. MacCORQUODALE, F. H. STODOLA, J. L. WACHTEL, R. D. COGHILL, W. C. RISSER, J. E. PHILIP, O. TOUSTER
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f05a12cb9f51759768b9b93d09570133
https://doi.org/10.2307/j.ctt183px0j.8
https://doi.org/10.2307/j.ctt183px0j.8
Publikováno v:
Journal of Child and Family Studies. 7:171-186
We examined the relationship between several characteristics of parents' narrative productions and two measures of maladaptive parenting. The two maladaptive parenting variables, indiscriminate responding to children's behavior and parent compliance
Publikováno v:
Journal of Biological Chemistry. 266:16876-16885
Rat liver alpha-mannosidase II, a hydrolase involved in the processing of asparagine-linked oligosaccharides, is an integral membrane glycoprotein facing the lumen of Golgi membranes. We have previously shown (Moremen, K. W., and Touster, O. (1986) J
Publikováno v:
The Journal of Cell Biology
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
alpha-mannosidases I and II (Man I and II) are resident enzymes of the Golgi complex involved in oligosaccharide processing during N-linked glycoprotein biosynthesis that are widely considered to be markers of the cis- and medial-Golgi compartments,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4809b937aa2bc050e2d9911c5bf59c1
https://idus.us.es/xmlui/handle/11441/40571
https://idus.us.es/xmlui/handle/11441/40571
Publikováno v:
The Journal of biological chemistry. 266(25)
Rat liver alpha-mannosidase II, a hydrolase involved in the processing of asparagine-linked oligosaccharides, is an integral membrane glycoprotein facing the lumen of Golgi membranes. We have previously shown (Moremen, K. W., and Touster, O. (1986) J
Autor:
O Touster, L D Strawser
Publikováno v:
Journal of Biological Chemistry. 254:3716-3719
A binding protein with apparent specificity for beta-glucuronidase has been partially purified from a Triton X-100 extract of rat liver microsomes by affinity chromatography on glucuronidase-Sepharose 2B. It appears that once removed from the membran
Publikováno v:
Journal of Biological Chemistry. 257:9991-10000
Rat liver glucosidase II, an endoplasmic reticulum hydrolase involved in the biosynthesis of the N-linked class of glycoproteins, has been purified in good yield to a state approaching homogeneity. The purified enzyme hydrolyzes p-nitrophenyl-alpha-D
Autor:
D J Opheim, O Touster
Publikováno v:
Journal of Biological Chemistry. 253:1017-1023
Rat liver contains alpha-D-mannosidases in lysosomes, Golgi membranes, and cytosol. The lysosomal enzyme has now been purified approximately 30,000-fold over the crude extract and is free of at least 13 other lysosomal hydrolases. The enzyme has an a
Autor:
O. Touster, D. R. P. Tulsiani
Publikováno v:
Journal of Biological Chemistry. 262:6506-6514
Swainsonine is a potent inhibitor of lysosomal alpha-D-mannosidase, causes the production of hybrid glycoproteins, and is reported to produce a phenocopy of hereditary alpha-mannosidosis. We now report that the effects of swainsonine administration i
Publikováno v:
Journal of Biological Chemistry. 250:4770-4776
Beta-Glucuronidase isolated from the preputial gland of the female rat has previously been shown to be a tetrameric glycoprotein. We have now separated the enzyme into several molecular forms by chromatography on hydroxylapatite columns. The three ma