Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Richard B. Jennett"'
Publikováno v:
Biochemical pharmacology. 44(1)
We have shown previously that acetaldehyde forms stable covalent adducts with tubulin, resulting in impaired microtubule formation. The present study explored the mechanism responsible for impaired microtubule formation caused by the substoichiometri
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 544:144-152
The effects of phenobarbital on protein and glycoprotein synthesis and secretion were studied in rat liver slices. Phenobarbital (2 mM) decreased [14C]glucosamine and [14C]leucine incorporation into liver proteins and markedly inhibited their incorpo
Publikováno v:
Life Sciences. 45:1461-1466
The regulatory protein, calmodulin, undergoes major conformational changes in response to changes in intracellular calcium concentration. Furthermore, calmodulin has been reported to have lysine residues which markedly increase their reactivity towar
Publikováno v:
Hepatology. 1:590-598
The effects of ethanol on the synthesis and secretion of serum glycoproteins and albumin, a nonglycosylated protein, were studied in rat liver slices. Serum glycoproteins and albumin were determined by immunoprecipitation from either the incubation m
Publikováno v:
Archives of Biochemistry and Biophysics. 204:181-190
Colchicine-binding properties of the total cytoplasmic pool of tubulin from rat liver were evaluated in tubulin-stabilizing (TS) supernates. Microtubules were separated from free tubulin using a microtubule-stabilizing solution (MTS) and ultracentrif
Publikováno v:
Pharmacology. 21:363-368
Ethanol, acetaldehyde, and acetate were investigated for their effects on bovine neurotubulin polymerization. Ethanol at concentrations as high as 50 mM did not affect the rate or extent of tubulin polymerization. Acetyldehyde inhibited tubulin polym
Publikováno v:
Hepatology. 7:787-789
Immunization of mice with acetaldehyde conjugated to human plasma proteins resulted in the production of polyclonal antibodies that reacted with erythrocyte protein-acetaldehyde conjugates, but not with control erythrocyte proteins. Such antibodies r
Publikováno v:
Annals of the New York Academy of Sciences. 492
Acetaldehyde covalently binds to purified tubulin in vitro to form both stable and unstable adducts. The formation of stable adducts can be greatly facilitated by the inclusion of the relatively gentle and Schiff base specific reducing agent, sodium
Publikováno v:
Molecular and Cellular Biochemistry. 71
The effects of the microtubular inhibitor, podophyllotoxin, on mitochondrial respiration were determined using isolated, digitonin-permeabilized hepatocytes and isolated mitochondria. In hepatocytes, podophyllotoxin (1.5 mM) inhibited coupled and unc
Publikováno v:
Archives of biochemistry and biophysics. 256(1)
The covalent binding of [14C]acetaldehyde to purified beef brain tubulin was characterized. As we have found for several other proteins, tubulin bound acetaldehyde to form both stable and unstable adducts. Unstable adducts (Schiff bases) were stabili