Luteinizing hormone. I. Circular dichroism and spectrophotometric titration of porcine and bovine hormones and of their alpha and beta subunits.
Explore the source record for details and available documents.
Amino Acid Sequence↗
Biomedical subjects
Y Combarnous
Publications and source records attributed to Y Combarnous.
Luteinizing hormone. 2. Relative reactivities of tyrosyl residues of the porcine hormone towards iodination.
Explore the source record for details and available documents.
Amino Acid Sequence↗
Proceedings: The disulphide bridges of porcine luteinizing hormone alpha subunit.
Explore the source record for details and available documents.
Amino Acid Sequence↗
Proceedings: Binding of luteinizing hormone to functional collagenase-isolated testicular interstitial cells.
Explore the source record for details and available documents.
Animals↗
The primary structure of the porcine luteinizing-hormone alpha-subunit.
Explore the source record for details and available documents.
Amino Acid Sequence↗
[Primary structure of the subunits of luteinizing hormone (LH); a comparison of amino acid sequence of the alpha and beta chains of LH of ovine, bovine, procine and human origin].
Explore the source record for details and available documents.
Amino Acid Sequence↗
Porcine luteinizing hormone. The amino acid sequence of the alpha subunit.
Explore the source record for details and available documents.
Journal Article↗
Role of a regulating protein and molecular oxygen in the mechanism of action of luteinizing hormone.
Explore the source record for details and available documents.
Animals↗
Purification and characterization of luteinizing hormone from the dromedary (Camelus dromedarius).
Luteinizing hormone (LH) has been purified from 150 dromedary pituitaries and its partial physicochemical, biological and immunological characterization has been achieved. Purification of the hormone was monitored by a porcine LH radioreceptor assay (RRA). In this system, the final camLH preparation exhibited an activity 0.6-fold that of highly purified porcine LH. The acid half-dissociation of camLH at equilibrium was observed at pH 4.2. A homologous camLH RRA was developed using the testicular plasma membrane fraction from prepubertal camels and radioiodinated, highly-purified camLH. Pituitary and chorionic gonadotropins (CG) from several mammalian species were compared to camLH in this system. The equine gonadotropins eLH and eCG were shown to be 6 times less potent in the camel RRA than in the porcine RRA, whereas the LH from other species exhibited similar activities in both systems. This particularity of camel LH receptors offers a new tool for the study of structural features of gonatropin interactions with their receptors.
Animals↗