MOLECULAR-BASIS OF LOW-TEMPERATURE SENSITIVITY IN PIG HEMOGLOBINS

S Condo; M Corda; M Sanna; M Pellegrini; M Ruiz; Massimo Castagnola; Bruno Giardina

doi:10.1111/j.1432-1033.1992.tb17347.x

MOLECULAR-BASIS OF LOW-TEMPERATURE SENSITIVITY IN PIG HEMOGLOBINS

S Condo, M Corda, M Sanna, M Pellegrini, M Ruiz, Massimo Castagnola, Bruno Giardina

Università Cattolica del Sacro Cuore

Research output: Contribution to journal › Article

11 Citations (Scopus)

Abstract

It has been generally assumed that mammals have blood with a greater temperature sensitivity than ectothermic organisms. Recent results have shown that in some species of mammals, Hb displays a value of overall oxygenation enthalpy (AH) much less exothermic than that observed for most mammalian hemoglobins, including human adult Hb. In this respect, a very interesting case is represented by porcine blood which shows a modest effect of temperature, the temperature coefficient of its oxygen-dissociation curve being significantly lower than that of human blood. Here we report a detailed functional characterization of pig Hb, which, interpreted on the basis of the amino acid sequence of the alpha and beta chains of the molecule, sheds some light on the molecular basis of the phenomenon.

Original language	English
Pages (from-to)	773-776
Number of pages	4
Journal	European Journal of Biochemistry
Volume	209
DOIs	https://doi.org/10.1111/j.1432-1033.1992.tb17347.x
Publication status	Published - 1992

Keywords

HEMOGLOBINS

Access to Document

10.1111/j.1432-1033.1992.tb17347.x

Cite this

@article{e4748d12b5f74c1ab21f54a46c6bb76c,

title = "MOLECULAR-BASIS OF LOW-TEMPERATURE SENSITIVITY IN PIG HEMOGLOBINS",

abstract = "It has been generally assumed that mammals have blood with a greater temperature sensitivity than ectothermic organisms. Recent results have shown that in some species of mammals, Hb displays a value of overall oxygenation enthalpy (AH) much less exothermic than that observed for most mammalian hemoglobins, including human adult Hb. In this respect, a very interesting case is represented by porcine blood which shows a modest effect of temperature, the temperature coefficient of its oxygen-dissociation curve being significantly lower than that of human blood. Here we report a detailed functional characterization of pig Hb, which, interpreted on the basis of the amino acid sequence of the alpha and beta chains of the molecule, sheds some light on the molecular basis of the phenomenon.",

keywords = "HEMOGLOBINS, HEMOGLOBINS",

author = "S Condo and M Corda and M Sanna and M Pellegrini and M Ruiz and Massimo Castagnola and Bruno Giardina",

year = "1992",

doi = "10.1111/j.1432-1033.1992.tb17347.x",

language = "English",

volume = "209",

pages = "773--776",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Blackwell Science Limited:PO Box 88, Oxford OX2 0NE United Kingdom:011 44 1865 776868, 011 44 1865 206038, EMAIL: [email protected], INTERNET: http://www.blackwell-science.com, Fax: 011 44 1865 721205",

}

TY - JOUR

T1 - MOLECULAR-BASIS OF LOW-TEMPERATURE SENSITIVITY IN PIG HEMOGLOBINS

AU - Condo, S

AU - Corda, M

AU - Sanna, M

AU - Pellegrini, M

AU - Ruiz, M

AU - Castagnola, Massimo

AU - Giardina, Bruno

PY - 1992

Y1 - 1992

N2 - It has been generally assumed that mammals have blood with a greater temperature sensitivity than ectothermic organisms. Recent results have shown that in some species of mammals, Hb displays a value of overall oxygenation enthalpy (AH) much less exothermic than that observed for most mammalian hemoglobins, including human adult Hb. In this respect, a very interesting case is represented by porcine blood which shows a modest effect of temperature, the temperature coefficient of its oxygen-dissociation curve being significantly lower than that of human blood. Here we report a detailed functional characterization of pig Hb, which, interpreted on the basis of the amino acid sequence of the alpha and beta chains of the molecule, sheds some light on the molecular basis of the phenomenon.

AB - It has been generally assumed that mammals have blood with a greater temperature sensitivity than ectothermic organisms. Recent results have shown that in some species of mammals, Hb displays a value of overall oxygenation enthalpy (AH) much less exothermic than that observed for most mammalian hemoglobins, including human adult Hb. In this respect, a very interesting case is represented by porcine blood which shows a modest effect of temperature, the temperature coefficient of its oxygen-dissociation curve being significantly lower than that of human blood. Here we report a detailed functional characterization of pig Hb, which, interpreted on the basis of the amino acid sequence of the alpha and beta chains of the molecule, sheds some light on the molecular basis of the phenomenon.

KW - HEMOGLOBINS

UR - http://hdl.handle.net/10807/23560

U2 - 10.1111/j.1432-1033.1992.tb17347.x

DO - 10.1111/j.1432-1033.1992.tb17347.x

M3 - Article

SN - 0014-2956

VL - 209

SP - 773

EP - 776

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

ER -

MOLECULAR-BASIS OF LOW-TEMPERATURE SENSITIVITY IN PIG HEMOGLOBINS

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this