Zobrazeno 1 - 10
of 266
pro vyhledávání: ''
Publikováno v:
Biochemical Journal. 439:227-233
The hOCTN1 (human organic cation transporter 1) overexpressed in Escherichia coli and purified by Ni-chelating chromatography has been reconstituted in liposomes by detergent removal with a batch-wise procedure. The reconstitution was optimized with
Publikováno v:
Biochemical Journal. 424:385-398
Gap junctions play important roles in auditory function and skin biology; mutations in the Cx26 (connexin26) gene are the predominant cause of inherited non-syndromic deafness and cause disfiguring skin disorders. Mass spectrometry (MS) was used to i
Autor:
Naila Ahmed, Paul J. Thornalley
Publikováno v:
Biochemical Journal. 364:15-24
Glycation of proteins leads to the formation of advanced glycation endproducts (AGEs) of diverse molecular structure and biological function. Serum albumin derivatives modified to minimal and high extents by methylglyoxal and glucose in vitro have be
Publikováno v:
Biochemical Journal. 364:1-14
Glycation of proteins leads to the formation of early glycation adducts (fructosamine derivatives) and advanced glycation endproducts (AGEs). Formation of AGEs has been linked to the development of cataract, diabetic complications, uraemia, Alzheimer
Autor:
Hans K. Erickson, Jack Kyte
Publikováno v:
Biochemical Journal. 336:443-449
A combination of vectorial modification and site-directed immunochemistry has been used to determine the disposition, with respect to the membrane, of Lys-691 of the anion exchanger from human erythrocytes. Intact erythrocytes and inside-out vesicles
Publikováno v:
Biochemical Journal. 330:1423-1431
An 80 kDa protein was purified from calf bone by HCl-demineralization followed by 0.5 M EDTA/1.0 M NaCl extraction and sequential chromatography on DE-52, hydroxyapatite, and TSK-gel G3000SW HPLC columns. From the DE-52 column the protein was eluted
Autor:
Antonio F. Hernández, Antonio Pla, Anabel Marina, Fernando Gil, Lourdes Rodrigo, Jesús Vázquez
Publikováno v:
Europe PubMed Central
ResearcherID
ResearcherID
Paraoxonase (paraoxon hydrolase), an enzyme that hydrolyses paraoxon (O,O-diethyl O-p-nitrophenyl phosphate), is located in mammals primarily in the serum and liver. Although considerable information is available regarding serum paraoxonase, little i
Autor:
Robert J. Beynon, Stephen P. Coburn, Deborah M. Leyland, Richard H.T. Edwards, Richard P. Evershed
Publikováno v:
Scopus-Elsevier
The majority of vitamin B6 in the body is in skeletal muscle, bound as the cofactor pyridoxal 5´-phosphate to one abundant protein, glycogen phosphorylase. Previous work has established that radiolabelled vitamin B6 can be used as a turnover label f
Publikováno v:
Biochemical Journal. 311:431-435
Human serum albumins modified by covalently bound tolmetin or zomepirac were synthesized as models for similar products formed in vivo from acyl glucuronides. Activated esters of both drugs were prepared with 1-ethyl-3-(3-dimethylaminopropyl)-carbodi
Publikováno v:
Biochemical Journal. 311:233-238
Proteoglycans (PGs), biosynthetically labelled with [35S]sulphate, were isolated from mouse mastocytoma tissue. Chromatography on antithrombin (AT)-Sepharose resulted in the separation of the 35S-labelled PGs into three fractions: PGs with no affinit