Hemoglobin

Name: Hemoglobin
Brand: Springer-Verlag Berlin and Heidelberg GmbH & Co. KG
SKU: 9783642808036
Price: 551.94 RON
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Cooperativity and Electronic Properties

Autor: M. Weissbluth

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Legare: Carte broșată

Editura: Springer-Verlag Berlin and Heidelberg GmbH & Co. KG

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Approximately one third of the mass of a mammalian red blood cell is hemo globin. Its major function...

Informații despre carte

Autor

M. Weissbluth

Limbă

engleză

Legare

Carte - Carte broșată

Publicat

2011

Pagini

176

EAN

9783642808036

ISBN

9783642808036

Enbook ID

06622155

Editura

Springer-Verlag Berlin and Heidelberg GmbH & Co. KG

Greutate

314

Dimensiuni

156 x 244 x 11

Descriere completă

Approximately one third of the mass of a mammalian red blood cell is hemo globin. Its major function is to bind oxygen at the partial pressure prevailing in the lungs and to release it to the tissues where the partial pressure is lower. The process whereby hemoglobin performs this essential physiological role is characterized by a cooperative interaction among its constituent subunits. A great deal of research effort has been devoted to this interaction, going back at least as far as the fitst decade of this century. Moreover, cooperativity in hemo globin is probably not unique; it may well be one instance of a general class of interactions that occur in biological molecules. Certain enzymes with a variety of regulatory and catalytic functions, for example, contain several sites which interact in a highly specific manner such that the affinity of a given site for the substrate is markedly influenced by the state of binding at the other sites. But whereas we know very little of the structure of most enzymes of this type, hemo globin is one of a very small number of biological molecules whose immensely intricate machinery has been revealed to us. We owe this insight to the group under the leadership of M. F. PERUTZ in Cambridge, England, whose research over a period of several decades culminated in a detailed description of the three dimensional structure.

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Hemoglobin

Cooperativity and Electronic Properties

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