Results 261 to 270 of about 210,654 (311)
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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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Glycoconjugate Journal, 1997
Glycoproteins are a diverse group of complex macromolecules that are present in virtually all forms of life. Their presence in prokaryotes, however, has been demonstrated, and accepted, only recently. Bacterial glycoproteins have been identified in many archaeobacteria and in eubacteria.
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Glycoproteins are a diverse group of complex macromolecules that are present in virtually all forms of life. Their presence in prokaryotes, however, has been demonstrated, and accepted, only recently. Bacterial glycoproteins have been identified in many archaeobacteria and in eubacteria.
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Viral glycoproteins are found decorating mainly enveloped viruses and to a lesser extent non-enveloped ones. During virus morphogenesis the virion's external proteins may undergo posttranslational modifications such as the addition of sugar moieties at specific amino acids, thus becoming glycosylated.
Soledad, Stagnoli, Nicola G A, Abrescia
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Soledad, Stagnoli, Nicola G A, Abrescia
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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
openaire +2 more sources