Search Results - "PEKAR, A. H"

Altering the association properties of insulin by amino acid replacement by Brems, D N, Alter, L A, Beckage, M J, Chance, R E, DiMarchi, R D, Green, L K, Long, H B, Pekar, A H, Shields, J E, Frank, B H

“…The importance of ProB28 and LysB29 on the self-association of insulin was established by systematically truncating the C terminus of the B chain. The…”
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Effects of non-covalent self-association on the subcutaneous absorption of a therapeutic peptide by CLODFELTER, D. K, PEKAR, A. H, REBHUN, D. M, DESTRAMPE, K. A, HAVEL, H. A, MYERS, S. R, BRADER, M. L

“…To utilize an acylated peptide as a model system to investigate the relationships among solution peptide conformation, non-covalent self-association,…”
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Evidence for a self-associating equilibrium intermediate during folding of human growth hormone by DeFelippis, Michael R, Alter, Leila A, Pekar, Allen H, Havel, Henry A, Brems, David N

“…It has been previously shown, by equilibrium denaturation, that human growth hormone (hGH) folds by a cooperative two-state process. This is in contrast to the…”
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Acid stabilization of insulin by Bryant, Christopher, Spencer, Donald B, Miller, Alita, Bakaysa, Diane L, McCune, Karen S, Maple, Steven R, Pekar, Allen H, Brems, David N

“…The effect of pH on the conformational stability of insulin was studied. Surprisingly, the Gibbs free energy of unfolding increased approximately 30% by…”
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Hypoglycemic potency and metabolic clearance rate of intravenously administered human proinsulin and metabolites by Tillil, H, Frank, B H, Pekar, A H, Broelsch, C, Rubenstein, A H, Polonsky, K S

“…Since circulating proinsulin has been suggested to be important in the pathogenesis of noninsulin-dependent diabetes, and biosynthetic human proinsulin (HPI)…”
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Effect of salts on the structure of a potent analog of growth hormone releasing hormone as determined by optical spectroscopy by Needham, G F, Pekar, A H, Havel, H A

“…Optical spectroscopic methods (circular dichroism, analytical ultracentrifugation, and static light scattering) were employed to study the solution behavior of…”
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Detection of an equilibrium intermediate in the folding of a monomeric insulin analog by Bryant, Christopher, Strohl, Margaret, Green, L. Kenney, Long, Harlan B, Alter, Leila A, Pekar, Alan H, Chance, Ronald E, Brems, David N

“…To determine the conformational properties of the C-terminal region of the insulin B-chain relative to the helical core of the molecule, we have investigated…”
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Physical studies on proinsulin. Comparison of the titration behavior of the tyrosine residues in insulin and proinsulin by Frank, B. H, Veros, A. J, Pekar, A. H

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Insulin and proinsulin conformation in solution by Frank, B H, Pekar, A H, Veros, A J

“…The physical chemistry of the insulin molecule in solution is reviewed. The nature of the self-association behavior is such that at physiological concentration…”
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Physicochemical basis for the rapid time‐action of LysB28ProB29‐insulin: Dissociation of a protein‐ligand complex by Bakaysa, Diane L., Radziuk, Jerry, Havel, Henry A., Brader, Mark L., Li, Shun, Dodd, Steven W., Beals, John M., Pekar, Allen H., Brems, David N.

“…The rate‐limiting step for the absorption of insulin solutions after subcutaneous injection is considered to be the dissociation of self‐associated hexamers to…”
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Physical Properties of Nitroglucagons and Aminoglucagons by Frank, Bruce H., Pekar, Allen H.

“…Mononitroglucagon (NO2 group on tyrosine residue 13) exhibits physical properties very similar to those of unmodified glucagon. The far ultraviolet CD spectra…”
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Isolation and characterization of a genetic variant of bovine proinsulin by Frank, B H, Pekar, A H, Pettee, J M, Schirmer, E M, Johnson, M G, Chance, R E

“…A genetic variant of bovine proinsulin has been isolated using preparative reverse-phase HPLC. The new proinsulin (bovine proinsulin II) differs from the known…”
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Conformation of proinsulin. Comparison of insulin and proinsulin self-association at neutral pH by Pekar, Allen H, Frank, Bruce H

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Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association by Sukumar, Muppalla, Doyle, Brandon L, Combs, Jessica L, Pekar, Allen H

“…Therapeutic antibodies are often formulated at a high concentration where they may have an opalescent appearance. The aim of this study is to understand the…”
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Crystalline L-asparaginase from Escherichia coli B. II. Physical properties, subunits, and reconstitution behavior by Frank, B H, Pekar, A H, Veros, A J, Ho, P P

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Glucagon structure and function. I. Purification and properties of bovine glucagon and monodesmidoglucagon by Bromer, W W, Boucher, M E, Patterson, J M, Pekar, A H, Frank, B H

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On-line data acquisition from the ultracentrifuge by Pekar, A H, Weller, R E, Byers, R A, Frank, B H

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Hybrid insulin cocrystals for controlled release delivery by Brader, Mark L, Myers, Sharon R, Sukumar, Muppalla, Pekar, Allen H, McClellan, David S, Chance, Ronald E, Flora, David B, Cox, Amy L, Irwin, Lynnie

“…The ability to tailor the release profile of a drug by manipulating its formulation matrix offers important therapeutic advantages. We show here that human…”
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Biophysical signatures of noncovalent aggregates formed by a glucagonlike peptide-1 analog: a prototypical example of biopharmaceutical aggregation by Doyle, Brandon L, Pollo, Mark J, Pekar, Allen H, Roy, Michael L, Thomas, Beth Ann, Brader, Mark L

“…LY307161 is a 31 amino acid analog of glucagonlike peptide-1(7-37)OH susceptible to physical instability associated with pharmaceutical processing. Orthogonal…”
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