The interaction of heparin/polyanions with bovine, porcine, and human growth hormone.

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Abstract Text:

The interaction of polyanions with proteins is of potential pharmaceutical and cellular significance. A partial thermodynamic description of the interaction of four representative polyanions with human, bovine, and porcine growth hormone is described. A heparin bead-binding assay confirms all growth hormones bind to heparin but to varying extents. Moderate-binding constants and high ratios of bound protein to the more extended polyanions, heparin, and dextran sulfate were measured by isothermal titration calorimetry and dynamic light scattering. The binding constants and ratio of protein bound to ligand were significantly smaller for the low molecular weight polyanions phytic acid and sucrose octasulfate (SOS). The effect of polyanion binding on the bovine, porcine, and human growth hormone's (hGH) structural and colloidal stability was also explored. Heparin and dextran sulfate inhibit porcine somatotropin (pST) and bovine somatotropin (bST) aggregation to the greatest extent, as compared to phytic acid and SOS, while decreasing secondary and tertiary structural stability as measured by the temperature dependence of their circular dichroism and intrinsic fluorescence. Somewhat surprisingly, the polyanions do not appear to affect the structure or stability of hGH. The potential biological significance of growth hormone polyanion interactions is discussed. (c) 2007 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 97:1368-1385, 2008.

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Publishing Authors By Initials

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of pharmaceutical sciences

VOLUME: 97

Page Numbers: 1368-85

Journal Abbreviation:

ISSN: 0022-3549

DAY: 4

MONTH: Apr

YEAR: 2008

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985195

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for The interaction of heparin/polyanions with bovine, porcine, and human growth hormone.

AFFILIATION: Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Pharm Sci

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone Related Publications

• A Review of: Vaccine Adjuvants and Delivery Systems.
• A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams.
• A network-based analysis of polyanion-binding proteins utilizing human protein arrays.
• A network-based analysis of polyanion-binding proteins utilizing yeast protein arrays.
• A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine.
• A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine.
• Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: effects of ligand binding.
• Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants.
• Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability.
• Intravenous cocaine self-administration: individual differences in male and female C57BL/6J mice.
• Linked outbreaks of hepatitis A in homosexual men and in food service patrons and employees.
• Pandemic influenza preparedness and community resiliency.
• Periadolescent nicotine exposure reduces cocaine reward in adult mice.
• Physical characterization of clostridium difficile toxins and toxoids: effect of the formaldehyde crosslinking on thermal stability.
• Physical stabilization of norwalk virus-like particles.
• Positions of authority may equal lawsuits.
• Preformulation studies of Clostridium difficile toxoids A and B.
• Side effects of diphtheria-tetanus toxoid in adults.
• Spectroscopic methods for the physical characterization and formulation of nonviral gene delivery systems.
• Stabilization of measles virus for vaccine formulation.
• Stabilization of proteins by recombinant human gelatins.
• The analysis of protein pharmaceuticals: near future advances.
• The complex inter-relationships between protein flexibility and stability.
• The interaction of heparin/polyanions with bovine, porcine, and human growth hormone.
• The structure, stability, and complex behavior of recombinant human gelatins.
• pH sensitivity of type III secretion system tip proteins.