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Proceedings of the Royal Society of London. Series B. Biological Sciences, 1967
Abstract Our first investigations of the action of lysozyme on tetrasaccharides isolated from chitin showed that lysozyme, like many other known glycosides, is a transferase. Under certain conditions (oligosaccharide concentration 1 to 2%, the enzyme concentration 0.5%) the synthetic process may yield an insoluble chitin-like product.
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Abstract Our first investigations of the action of lysozyme on tetrasaccharides isolated from chitin showed that lysozyme, like many other known glycosides, is a transferase. Under certain conditions (oligosaccharide concentration 1 to 2%, the enzyme concentration 0.5%) the synthetic process may yield an insoluble chitin-like product.
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2000
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate. Most GSTs are located in the cytosol,
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Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate. Most GSTs are located in the cytosol,
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Inhibitors of prenyl transferases
Current Opinion in Oncology, 1997Because farnesylation of Ras is required for its cancer-causing activity, several classes of farnesyl transferase inhibitors have recently been developed as potential anticancer drugs. During the last 12 months, important advances have been made in this field.
S, Sebti, A D, Hamilton
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Mosquito Glutathione Transferases
2005The glutathione transferases (glutathione S-transferases, GSTs) are a diverse family of enzymes involved in a wide range of biological processes, many of which involve the conjugation of the tripeptide glutathione to an electrophilic substrate. Relatively little is known about the endogenous substrates of mosquito GSTs, and most studies have focused on
Hilary, Ranson, Janet, Hemingway
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Measurement of Glutathione Transferases
Current Protocols in Toxicology, 2002AbstractThere are multiple glutathione transferase genes, the proteins for which have different substrate specificities. The various genes are differentially expressed such that species and organs and tissues differ qualitatively and quantitatively for cytosolic and membrane‐bound forms. This unit provides protocols for analysis of transferase activity
B, Mannervik, P, Jemth
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Critical Reviews in Clinical Laboratory Sciences, 2001
Serum gamma-glutamyl transferase (GGT) has been widely used as an index of liver dysfunction and marker of alcohol intake. The last few years have seen improvements in these areas and advances in understanding of its physiological role in counteracting oxidative stress by breaking down extracellular glutathione and making its component amino acids ...
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Serum gamma-glutamyl transferase (GGT) has been widely used as an index of liver dysfunction and marker of alcohol intake. The last few years have seen improvements in these areas and advances in understanding of its physiological role in counteracting oxidative stress by breaking down extracellular glutathione and making its component amino acids ...
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Farnesyl Transferase Inhibitors
Cancer Investigation, 2007Substituted imidazoles and thiazoles having the formula are useful for inhibiting farnesyltransferase. Also disclosed are farnesyltransferase-inhibiting compositions and methods of inhibiting farnesyltransferase in a patient.
Tianhong, Li, Joseph A, Sparano
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Transesterification by Peptidyl Transferase
Nature, 1970Peptidyl transferase, the enzyme which catalyses formation of peptide bonds, can be stimulated by CCA, the 3′-terminus of tRNA, to catalyse also a transesterification reaction involving nucleophilic attack of Met-tRNAfMet by ethanol to yield fMet-ethyl ester.
E, Scolnick +3 more
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1996
Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
A, Raha, K D, Tew
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Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
A, Raha, K D, Tew
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Peptidyl transferase and beyond
Biochemistry and Cell Biology, 1995The peptidyl transferase center of the Escherichia coli ribosome encompasses a number of 50S-subunit proteins as well as several specific segments of the 23S rRNA. Although our knowledge of the role that both ribosomal proteins and 23S rRNA play in peptide bond formation has steadily increased, the location, organization, and molecular structure of ...
Wower, J +5 more
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