Preparation of unaltered hemoglobin from human placentas for possible use in blood substitutes.
Identifieur interne : 003865 ( Main/Exploration ); précédent : 003864; suivant : 003866Preparation of unaltered hemoglobin from human placentas for possible use in blood substitutes.
Auteurs : G. Fasan [France] ; M. Grandgeorge ; C. Vigneron ; Édith DellacherieSource :
- Journal of biochemical and biophysical methods [ 0165-022X ]
Descripteurs français
- KwdFr :
- MESH :
- isolement et purification : Hémoglobines.
- pharmacologie : Arginine, Carboxypeptidases.
- physiologie : Plasma sanguin.
- sang : Oxygène.
- Adulte, Carboxypeptidase B, Humains, Hémoglobine A, Hémoglobines, Liaison aux protéines, Placenta, Substituts sanguins.
English descriptors
- KwdEn :
- MESH :
- chemical , blood : Oxygen.
- chemical , chemistry : Blood Substitutes, Hemoglobins.
- chemical , drug effects : Hemoglobin A.
- chemical , isolation & purification : Hemoglobins.
- chemical , pharmacology : Arginine, Carboxypeptidases.
- chemistry : Placenta.
- physiology : Plasma.
- Adult, Carboxypeptidase B, Humans, Protein Binding.
Abstract
Hemoglobin extracted from human placentas could be used as the basis of blood substitutes provided it could be prepared on a large scale with appropriate oxygen-binding properties. Unfortunately, the industrial conditions under which it is extracted, produce hemoglobin with high oxygen affinity and which is no longer influenced by the classical effectors. These characteristics were shown to be caused by a degradation of the alpha-chain brought about by an arginine carboxypeptidase present in the placental tissues and leading to the disappearance of the C-terminal arginine residue. This carboxypeptidase which is released from the tissues during the process of crushing the frozen placentas, degrades the protein during the chromatographic purification procedure. The addition of an inhibitor of this carboxypeptidase (for example, arginine) as soon as the placentas are thawed and during the chromatographic process, makes it possible to obtain placental hemoglobin with oxygen-binding properties quite similar to those of HbA prepared from peripheral venous blood.
PubMed: 1918801
Affiliations:
Links toward previous steps (curation, corpus...)
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- to stream PubMed, to step Checkpoint: 000263
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Le document en format XML
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<term>Arginine (pharmacology)</term>
<term>Blood Substitutes (chemistry)</term>
<term>Carboxypeptidase B</term>
<term>Carboxypeptidases (pharmacology)</term>
<term>Hemoglobin A (drug effects)</term>
<term>Hemoglobins (chemistry)</term>
<term>Hemoglobins (isolation & purification)</term>
<term>Humans</term>
<term>Oxygen (blood)</term>
<term>Placenta (chemistry)</term>
<term>Plasma (physiology)</term>
<term>Protein Binding</term>
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<term>Arginine (pharmacologie)</term>
<term>Carboxypeptidase B</term>
<term>Carboxypeptidases (pharmacologie)</term>
<term>Humains</term>
<term>Hémoglobine A ()</term>
<term>Hémoglobines ()</term>
<term>Hémoglobines (isolement et purification)</term>
<term>Liaison aux protéines</term>
<term>Oxygène (sang)</term>
<term>Placenta ()</term>
<term>Plasma sanguin (physiologie)</term>
<term>Substituts sanguins ()</term>
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<front><div type="abstract" xml:lang="en">Hemoglobin extracted from human placentas could be used as the basis of blood substitutes provided it could be prepared on a large scale with appropriate oxygen-binding properties. Unfortunately, the industrial conditions under which it is extracted, produce hemoglobin with high oxygen affinity and which is no longer influenced by the classical effectors. These characteristics were shown to be caused by a degradation of the alpha-chain brought about by an arginine carboxypeptidase present in the placental tissues and leading to the disappearance of the C-terminal arginine residue. This carboxypeptidase which is released from the tissues during the process of crushing the frozen placentas, degrades the protein during the chromatographic purification procedure. The addition of an inhibitor of this carboxypeptidase (for example, arginine) as soon as the placentas are thawed and during the chromatographic process, makes it possible to obtain placental hemoglobin with oxygen-binding properties quite similar to those of HbA prepared from peripheral venous blood.</div>
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