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Biochemical and Biophysical Research Communications, 1973
Abstract Human caeruloplasmin and α 1 -acid glycoprotein and bovine fetuin were tritiated by reductive methylation of the e-amino group of lysine residues. Tritiated caeruloplasmin retained its oxidase activity and molecular sieve chromatography of the labelled glycoproteins showed that reductive methylation did not significantly affect their ...
G, Gregoriadis, B E, Ryman
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Abstract Human caeruloplasmin and α 1 -acid glycoprotein and bovine fetuin were tritiated by reductive methylation of the e-amino group of lysine residues. Tritiated caeruloplasmin retained its oxidase activity and molecular sieve chromatography of the labelled glycoproteins showed that reductive methylation did not significantly affect their ...
G, Gregoriadis, B E, Ryman
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Archives for Dermatological Research, 1975
Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis.
K, Miyazaki, N, Otaki
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Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis.
K, Miyazaki, N, Otaki
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2009
Increasing numbers of studies are reporting the modification of prokaryotic proteins with novel glycans. These proteins are often associated with virulence factors of medically important pathogens. Herein, we describe the steps required to characterize prokaryotic glycoproteins by mass spectrometry, using flagellin isolated from Clostridium botulinum ...
Twine, Susan M. +2 more
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Increasing numbers of studies are reporting the modification of prokaryotic proteins with novel glycans. These proteins are often associated with virulence factors of medically important pathogens. Herein, we describe the steps required to characterize prokaryotic glycoproteins by mass spectrometry, using flagellin isolated from Clostridium botulinum ...
Twine, Susan M. +2 more
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ChemInform, 2003
AbstractFor Abstract see ChemInform Abstract in Full Text.
P, Messner, C, Schäffer
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AbstractFor Abstract see ChemInform Abstract in Full Text.
P, Messner, C, Schäffer
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Archives of Microbiology, 1997
Rather recently it has become clear that prokaryotes (Archaea and Bacteria) are able to glycosylate proteins. A literature survey revealed the different types of glycoproteins. They include mainly surface layer (S-layer) proteins, flagellins, and polysaccharide-degrading enzymes. Only in a few cases is structural information available.
S, Moens, J, Vanderleyden
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Rather recently it has become clear that prokaryotes (Archaea and Bacteria) are able to glycosylate proteins. A literature survey revealed the different types of glycoproteins. They include mainly surface layer (S-layer) proteins, flagellins, and polysaccharide-degrading enzymes. Only in a few cases is structural information available.
S, Moens, J, Vanderleyden
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Disorders of glycoprotein degradation
Journal of Inherited Metabolic Disease, 1990SummaryThe intracellular degradation of glycoproteins occurs predominantly in the lysosomes through the concerted action of proteases and glycosidases. Genetic defects in any of the enzymes cleaving the oligosaccharide side chains lead to specific diseases because of an excessive lysosomal accumulation of partially degraded material, mostly ...
M, Cantz, B, Ulrich-Bott
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2019
Fil: Couto, Paula Monserrat. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir.
Couto, Paula Monserrat +1 more
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Fil: Couto, Paula Monserrat. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir.
Couto, Paula Monserrat +1 more
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Characterization of Glycoproteins: Carbohydrate Structures of Glycoprotein Hormones
1986Gylcoproteins are a complex group of macromolecules that are widely distributed in nature. They are present virtually in all forms of life and are involved in important biological functions (Wagh and Bahl, 1981; Sharon and Liz, 1982; Kobata, 1984). The importance of the role that the carbohydrates play in the functions of glycoproteins has been fairly ...
O P, Bahl, P V, Wagh
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