Results 351 to 360 of about 1,068,824 (393)
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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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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 ...
Brenda E. Ryman, Gregory Gregoriadis
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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 ...
Brenda E. Ryman, Gregory Gregoriadis
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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.
Kazuhiro Miyazaki, Noriko Ohtaki
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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.
Kazuhiro Miyazaki, Noriko Ohtaki
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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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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, Jozef 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, Jozef Vanderleyden
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Biochemical and Biophysical Research Communications, 1975
[14C]Glucosamine is incorporated in vivo in mouse brain into the major protein species present in purified tubulin preparations when analyzed both by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by isoelectric focusing. The radioactivity incorporated into tubulin can be recovered as a mixture of glucosamine and galactosamine.
Michael L. Shelanski, Howard Feit
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[14C]Glucosamine is incorporated in vivo in mouse brain into the major protein species present in purified tubulin preparations when analyzed both by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by isoelectric focusing. The radioactivity incorporated into tubulin can be recovered as a mixture of glucosamine and galactosamine.
Michael L. Shelanski, Howard Feit
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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 ...
Premanand V. Wagh, Om P. Bahl
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Biological Reviews, 1968
Summary1. Although the classical models of biomembranes have emphasized the lipid and protein nature of these structures, a small quantity of carbohydrate is present as glycoprotein and glycolipid in animal cell membranes. In this article an attempt has been made to indicate that such carbohydrate materials should be considered in any complete model of
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Summary1. Although the classical models of biomembranes have emphasized the lipid and protein nature of these structures, a small quantity of carbohydrate is present as glycoprotein and glycolipid in animal cell membranes. In this article an attempt has been made to indicate that such carbohydrate materials should be considered in any complete model of
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1979
Since membrane glycoproteins have been implicated in many neurobiological processes and functions (see Chapters 7, 8, and 11), the mechanisms and regulation of biosynthesis of the oligosaccharide units have been of great interest to cell and neurobiologists during the past 20 years.
C. J. Waechter, M. G. Scher
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Since membrane glycoproteins have been implicated in many neurobiological processes and functions (see Chapters 7, 8, and 11), the mechanisms and regulation of biosynthesis of the oligosaccharide units have been of great interest to cell and neurobiologists during the past 20 years.
C. J. Waechter, M. G. Scher
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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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