✦ LIBER ✦

Analysis of the effects of chloride and 2,3-diphosphoglycerate on the cooperative binding of oxygen to hemoglobin

✍ Scribed by Walter J. Deal

Publisher: Wiley (John Wiley & Sons)
Year: 1975
Tongue: English
Weight: 512 KB
Volume: 14
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.1975.360140615

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

Analysis of experimental equilibrium constants for the oxygenation of hemoglobin leads to a plausible mechanism for the effect of pH and of chloride ions on cooperativity in hemoglobin. According to this mechanism, the structural changes responsible for cooperativity in chloride‐ and 2,3‐diphosphoglycerate‐free hemoglobin are affected only slightly by changes in pH, and the effect of chloride can be accounted for by sequential binding and release of chloride ions during oxygenation.

📜 SIMILAR VOLUMES

Effect of oxygen binding on the dielectr

Effect of oxygen binding on the dielectric properties of hemoglobin

✍ Peter Schlecht; Helmut Vogel; Adalbert Mayer 📂 Article 📅 1968 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 521 KB

The dielectric properties of horse hemoglobin have been investigated in the frequency range for 100 kcps to 15 Mcps at varying degrees of oxygenation. A linear dependence of the specific increment on the degree of oxygenation wae found under a variety of experimental conditions, the increment of oxy

Possible effects of 1011 Hz radiation on

Possible effects of 1011 Hz radiation on the oxygen affinity of hemoglobin

✍ D. K. Kondepudi 📂 Article 📅 1982 🏛 John Wiley and Sons 🌐 English ⚖ 754 KB

## Abstract When oxygen binds to one of the subunits of hemoglobin, the oxygen affinity of the other subunits is enhanced. This cooperative interaction of the subunits is initiated by the movement of the heme plane toward the proximal side when oxygen binds to the heme. This motion is transmitted t

Temperature dependence of the effects of

Temperature dependence of the effects of some monohydric alcohols on the oxygen affinity of hemoglobin: Determination and analysis of thermodynamic parameters

✍ Lorenzo Cordone; Antonio Cupane; Pier L. San Biagio; Eugenio Vitrano 📂 Article 📅 1981 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 527 KB

## Abstract We studied the effects of methanol, ethanol, __iso__‐propanol, and __n__‐propanol on the reaction of hemoglobin with oxygen at various temperatures. The analysis of the results in terms of the Monod‐Wyman‐Changeux model allowed determination of the overall contribution of the alcohols t

The effect of inhibitor binding on the s

The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease

✍ Matthew J. Todd; Ernesto Freire 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 337 KB 👁 2 views

The effects of the peptide inhibitor acetyl pepstatin on the structural stability of the HIV-1 protease have been measured by high sensitivity calorimetric techniques. At 25°C and pH 3.6, acetyl pepstatin binds to HIV-1 protease with an affinity of 1.6 ؋ 10 7 M -1 and an enthalpy of 7.3 ؎ 0.5 kcal/m

The Binding of rhBMP-2 to the Receptors

The Binding of rhBMP-2 to the Receptors of viable MC3T3-E1 Cells and the Question of Cooperativity

✍ M. Wiemann; H. M. Rumpf; D. Bingmann; H. P. Jennissen 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 127 KB 👁 2 views

Effect of some monohydric alcohols on th

Effect of some monohydric alcohols on the oxygen affinity of hemoglobin: Relevance of solvent dielectric constant and hydrophobicity

✍ Lorenzo Cordone; Antonio Cupane; Pier L. San Biagio; Eugenio Vitrano 📂 Article 📅 1980 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 27 KB 👁 1 views

In the caption of Fig. 4 (p. 1983), the third line should read "dielectric constant values at 21.8"C" instead of "dielectric constant values at 20°C."