Zobrazeno 1 - 10
of 16
pro vyhledávání: '"M J, Treuheit"'
Autor:
H. B. Halsall, M. J. Treuheit
Publikováno v:
Chromatographia. 37:144-148
The glycosylation patterns of multiglycosylated proteins reflect both the cellular control of glycosyl transferase activity and the local control of the transfer event. Little information is available concerning these mechanisms. Changes in glycosyla
Publikováno v:
Journal of Biological Chemistry. 268:13914-13919
(Na,K)-ATPase is an integral membrane protein responsible for maintaining the Na+ and K+ ion concentration gradients across the plasma membranes of cells. All active (Na,K)-ATPase preparations consist of two subunits, designated alpha and beta. The a
Publikováno v:
Preparative Biochemistry. 23:375-387
Covalent structural information on membrane proteins is not easily acquired since it is difficult to obtain pure membrane proteins in sufficient quantities. We have therefore examined the Bio-Rad 491 prep cell continuous elution electrophoresis appar
Publikováno v:
Chromatographia. 33:521-524
Wheat germ agglutinin (WGA) affinity chromatography was examined as a method for the purification of the glycosylated beta subunit from SDS solubilized (Na,K)-ATPase. This lectin, WGA, bound quantitatively all of the beta subunit from SDS solubilized
Autor:
M. J. Treuheit, H. B. Halsall
Publikováno v:
Chromatographia. 31:63-66
Cigarette smokers have a phthalate noncovalently bound to their serum orosomucoid. The phthalate, whose concentration is dependent on the number of cigarettes smoked, is tentatively identified as a metabolite of di-(2-ethylhexyl)-phthalate, a common
Autor:
M. J. Treuheit, H. B. Halsall
Publikováno v:
Chromatographia. 35:90-92
Little is known about the alterations that have occurred at the individual glycosylation sites in allergy patients or how these glycosylation patterns may change after anti-allergy treatments. Using reverse-phase HPLC, we have quantitated the glycofo
Publikováno v:
Pharmaceutical research. 18(3)
BDNF, a noncovalent homodimer, was modified by covalently attaching polyethylene glycol (PEG) with an average molecular weight of 20kDa to the N-terminal methionine. Stability of modified BDNF (PEG-BDNF) in aqueous solution was compared to BDNF after
Autor:
M. J. Treuheit, H. B. Halsall
Publikováno v:
Chromatographia. 31:478-480
The glycoforms contained within each glycosylation site of orosomucoid can be separated by reverse-phase HPLC without removal of the associated peptide or chemical derivatization. The chromatographic properties of the glycopeptides are dominated by t
Publikováno v:
Pharmaceutical research. 15(12)
Determine the effect of PEGylation on in-vitro degradation for recombinant human Megakaryocyte Growth and Development Factor (rHuMGDF) in the neutral pH range.Degradation products were characterized by cation-exchange HPLC, N-terminal sequencing and
Publikováno v:
Pharmaceutical research. 13(7)
The liquid stability of rhG-CSF was investigated after polyethylene glycol (PEG) with an average molecular weight of 6000 daltons was covalently attached to the N-terminal methionine residue.The conjugation methods chosen for modifying the N-terminal