Comparison of the thermal stability characteristics of native and deglycosylated ovine pituitary lutropin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1982.tb03044.x/fullpdf
Reference11 articles.
1. Receptor binding, biological, and immunological properties of chemically deglycosylated pituitary lutropin
2. Deglycosylation of ovine pituitary lutropin subunits: Effects on subunit interaction and hormone activity
3. Inhibition of hormone-induced cyclic AMP production and steroidogenesis in interstitial cells by deglycosylated lutropin
4. A Protein Binding Assay for Adenosine 3':5'-Cyclic Monophosphate
5. A Radioreceptor Assay for Follicle-Stimulating Hormone1
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1. Is there any physiological role for gonadotrophin oligosaccharide heterogeneity in humans?;Human Reproduction;2001-05
2. Intrinsic tryptophan fluorescence measurements suggest that polylactosaminyl glycosylation affects the protein conformation of the gelatin-binding domain from human placental fibronectin;European Journal of Biochemistry;1990-05
3. Structure-stability relationships in proteins: a guide to approaches to stabilizing enzymes;Advanced Drug Delivery Reviews;1990-01
4. Characterization of a thermostable LH-immunoreactive material from bovine pituitary gland;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1987-01
5. [56] Chemical deglycosylation of glycoprotein hormones;Methods in Enzymology;1985
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