Zobrazeno 1 - 10
of 86
pro vyhledávání: '"Om P. Bahl"'
Autor:
Dharam S. Dhindsa, Om P. Bahl
Recently, considerable attention has been focused on studies of membrane structure and function--involvement of cell surface components in intercellular interaction, in translocation of ligands and receptors across cell membranes, and in the immunolo
Publikováno v:
Molecular and Cellular Endocrinology. 146:39-48
Human choriogonadotropin is a heterodimeric glycoprotein hormone comprised of noncovalently associated alpha- and beta-subunits. Each of the subunits has two N-glycosyl chains. In our previous communication, we investigated the role of individual car
Publikováno v:
Biochemistry. 36:12355-12363
Analogs of human choriogonadotropin (hCG) lacking N-glycosyl chains at alpha52Asn and alpha78Asn were purified from the culture media of insect cells by immunoaffinity chromatography using a monoclonal antibody column. As previously reported, while a
Publikováno v:
Molecular and Cellular Endocrinology. 122:173-182
Human choriogonadotropin (hCG), according to its three dimensional structure as determined by X-ray diffraction, has three beta-hairpin loops each in the alpha and beta subunit designated as alpha 1, alpha 2 alpha 3 and beta 1 beta 2 and beta 3, resp
Autor:
Wenyong Chen, Om P. Bahl
Publikováno v:
Molecular and Cellular Endocrinology. 91:35-41
Using the polymerase chain reaction (PCR) technique, the cDNA fragment corresponding to the receptor coding region for residues 1–294 was prepared from rat lutropin receptor (LHR) cDNA and subsequently subcloned into Escherichia coli expression vec
Autor:
Om P. Bahl, Prem Seth
Publikováno v:
Molecular and Cellular Endocrinology. 80:105-114
The detergent-soluble extract of rat ovary plasma membranes contained a Gs protein of about 100 kDa as shown by its elution behavior on a Bio Gel A-1.5m column. However, the cell membranes exposed to hCG (37° C, 15 min) contained in addition a highe
Publikováno v:
Journal of Biological Chemistry. 266:4081-4087
The β-subunit of human choriogonadotropin (hCG) has two complex type N-linked and four O-linked carbohydrate chains. To further evaluate the specificity of the carbohydrate moiety on the hCG function, we have expressed hCG β subunit in the baculovi
Autor:
Qing-Xiang Shen, Om P. Bahl
Publikováno v:
Molecular and Cellular Endocrinology. 72:167-173
Although amino acid sequences of the alpha- and beta-subunits of human choriogonadotropin (hCG) are known, only limited information is available on the disease state hCG. We have examined the amino acid sequences of the alpha- and beta-subunits of hC
Publikováno v:
Molecular and cellular endocrinology. 150(1-2)
Of all the four N-glycosyl chains present in hCG, only one of them at alpha52Asn is located at the alpha/beta subunit interface and is crucial for the biological function of the hormone. The other three are exposed on the surface of the molecule and
Autor:
Kui Shao, Om P. Bahl
Publikováno v:
Molecular and cellular endocrinology. 127(2)
According to the X-ray diffraction, human choriogonadotropin has four beta-hairpin and two long loops, equally distributed in each of the alpha and beta subunits. Radical mutations such as the replacement of alpha 18Phe and alpha 74Phe with Thr in th