EFECTO BOHR DE LA HEMOGLOBINA PDF

Slideshare uses cookies to improve functionality and performance, and to provide you with relevant advertising. If you continue browsing the site, you agree to the use of cookies on this website. See our User Agreement and Privacy Policy. See our Privacy Policy and User Agreement for details.

Author:Vukinos Tezragore
Country:Argentina
Language:English (Spanish)
Genre:Business
Published (Last):7 June 2014
Pages:281
PDF File Size:3.38 Mb
ePub File Size:6.94 Mb
ISBN:929-2-32951-196-3
Downloads:74500
Price:Free* [*Free Regsitration Required]
Uploader:Tojar



Las subunidades proteicas se mantienen unidas mediante enlaces no covalentes y ocupan diferentes posiciones relativas en la desoxihemoglobina y la oxihemoglobina. Palabras clave: Efecto Bohr, Hemoglobina. Hemoglobin Hb is a globular protein located inside the erythrocytes which function is carry oxygen from the lungs to the tissue capillaries. Structurally, the Hb is a hetero-protein formed by two types of peptide chains, each of them attached to a prosthetic group called hemegroup, consisting of a complex of protoporphyrin IX and ferrous iron.

The protein subunits are held together by non-covalent bonds and they occupy different relative positions in oxyhemoglobin and deoxyhemoglobin. The deoxy form called tense form T , has low affinity by oxygen, the oxygen binding to the Hb causes a disruption of ionic and hydrogen bonding favoring the relaxed form R.

Oxygen binding to hemoglobin presents a sigmoidal curve of saturation which reflects the cooperative binding of oxygen due to the quaternary structure of hemoglobin.

The ability of hemoglobin to bind oxygen is reversibly modulated by the pressure of CO 2 pCO 2 , pH, and availability of 2,3-bisphosphoglycerate. Therefore, the release of oxygen from hemoglobin is intensified when the pH decreases or increases pCO 2 Bohr Effect.

On the other hand, regarding the porphyrins metabolism; the heme biosynthesis is performed in the liver and in the erythrocytes-producing cells in bone marrow; begins with the condensation of glycine and succinil-CoA. This reaction is catalyzed by ALA synthase. The porphyrin ring is formed by condensation of four molecules of porphobilinogen with the subsequent incorporation of the iron to form heme group.

The hemoproteins degradation occurs in the liver and spleen. The first stage in the degradation is the production of biliverdin, which is reduced to bilirubin. Bilirubin is transported to the liver where solubility increases with the glucuronic acid conjugation. The diglucuronide bilirubin is transported to the bile canaliculi which is hydrolyzed by intestinal bacteria and reduced to stercobilin.

Keywords: Bohr Effect, Hemoglobin. Abstract Hemoglobin Hb is a globular protein located inside the erythrocytes which function is carry oxygen from the lungs to the tissue capillaries.

HMT DATA BOOK BY KOTHANDARAMAN PDF

Cooperatividad

.

ZEROCALCARE LA PROFEZIA DELLARMADILLO PDF

Christian Bohr

.

Related Articles