Equine luteinizing hormone and its subunits. Isolation and physicochemical properties

Landefeld, Thomas D.; McShan, W. H.

doi:10.1021/bi00704a012

Cited by 17 publications

(3 citation statements)

References 23 publications

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“…This is best illustrated when comparing pituitary-derived equine (e)LH with placental eCG. These gonadotrophins have identical amino acid sequences (Bousfield et al 1987) and yet the carbohydrate contents for eLH and eCG have been established as 24 and 45% respectively (Landefeld & McShan, 1974; Moore & Ward, 1980). Further¬ more, striking species-specific differences exist in the structure of asparagine (N)-linked oligosaccharides found on any particular glycoprotein hormone (Green & Baenziger, 1988a,6).…”

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confidence: 99%

Expression and characterization of biologically active ovine FSH from mammalian cell lines

Mountford

Brandon²,

Adams³

1994

Journal of Molecular Endocrinology

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Stably transfected cell lines expressing the alpha subunit, beta subunit and alpha/beta heterodimer of ovine (o)FSH have been established following the transfection of Chinese hamster ovary cells with alpha and beta subunit cDNA expression vectors. In the absence of the alpha subunit, FSH beta subunit polypeptides were inefficiently secreted and displayed a short intracellular half-life, while free alpha subunits were readily secreted in the absence of the beta subunit. Cotransfection of oFSH alpha and beta subunit cDNAs led to heterodimer assembly and secretion. While alteration of the nucleotide sequence flanking the beta subunit AUG initiation codon did not appreciably enhance heterodimer biosynthesis and secretion, the replacement of the 5' untranslated and signal peptide-coding regions of the beta subunit cDNA with the corresponding sequences from an oGH cDNA clone was associated with a twofold increase in oFSH heterodimer secretion. The recombinant oFSH had a higher molecular weight than pituitary-derived oFSH, and was more acidic than the native hormone when analysed using isoelectric focusing, suggesting a greater degree of sialylation of the recombinant hormone. A comparison of the activities of the recombinant and native hormones in the porcine testis radioreceptor assay and in the in vitro Sertoli cell bioassay revealed that the recombinant oFSH displayed enhanced biological activity in the Sertoli cell assay when compared with the native hormone.

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Expression and characterization of biologically active ovine FSH from mammalian cell lines

Mountford

Brandon²,

Adams³

1994

Journal of Molecular Endocrinology

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“…LH and the chorionic gonadotropin of the horse are unique in that their (3-subunit is coded by a single gene; furthermore, the subunit is synthesized with a heavily sialylated C-terminal extension of 2 4 -28 amino acids [Bousfield et al, 1987;Stewart & Maher, 1991], which in the case of LH appears to be removed at the time of secretion [Shand et al, 1991]. Early work showed that each equine gonadotropin exists within the pituitary in an unusually wide variety of forms (isoforms) that differ primarily in the composition of the carbohydrate side chains [Landefeld & McShan, 1974]. Gonadotropin isoforms also differ in relative potency in various types of assay, e.g., RIA, bioassay, receptor assay, etc.…”

Section: Relevance Of Gonadotropinmentioning

confidence: 99%

The Nonpregnant Mare: A Review of Some Current Research and of the Last 25 Years of Endocrinology

Irvine

1995

Biology of Reproduction

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“…The subunits of human (Rathnam & Saxena, 1975;Shome & Parlow, 1974a,b), sheep (Grimek & McShan, 1974;Papkoff & Ekblad, 1970) and equine (Landefeld & McShan, 1974) follitropin (folliclestimulating hormone, FSH) have been isolated and characterized. Further, the primary amino acid sequences of the subunits of human follitropin have been determined (Rathnam & Saxena, 1975;Shome & Parlow, 1974a,b).…”

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Isolation and characterization of the subunits of bovine follitropin

Cheng¹

1978

Biochemical Journal

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Highly purified bovine follitropin was dissociated into its alpha- and beta-subunits after treatment with 1 M-propionic acid. The dissociated subunits were fractionated by chromatography on DEAE-cellulose and further purified by gel filtration on Sephadex G-100. The isolated alpha- and beta-subunits were biologically inactive, but their recombinants regenerated 80% of the follitropin activity. The alpha-subunit of bovine follitropin recombined with the beta-subunits of bovine lutropin and thyrotropin to regenerate 70% of lutropin and 50% of thyrotropin activities respectively. The beta-subunit of bovine follitropin recombined with the alpha-subunit of either bovine lutropin or thyrotropin to regenerate about 75% of follitropin activity. Recombinations were monitored by specific radioligand-receptor assays and polyacrylamide-gel electrophoresis. The elution volumes of the alpha- and beta-subunits of bovine follitropin after gel filtration on Sephadex G-100 were almost identical. The amino acid composition of bovine follitropin-alpha was low in histidine, arginine, isoleucine and leucine, but relatively high in lysine, threonine and glutamic acid. The bovine follitropin-beta contained one methionine residue and low amounts of histidine and phenylalanine, but relatively high in aspartic acid, threonine and glutamic acid. The N-terminal residues of the alpha- and beta-subunits of bovine follitropin were identified to be phenylalanine and glycine respectively.

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Equine luteinizing hormone and its subunits. Isolation and physicochemical properties

Cited by 17 publications

References 23 publications

Expression and characterization of biologically active ovine FSH from mammalian cell lines

Expression and characterization of biologically active ovine FSH from mammalian cell lines

The Nonpregnant Mare: A Review of Some Current Research and of the Last 25 Years of Endocrinology

Isolation and characterization of the subunits of bovine follitropin

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