Selective carboxymethylation of the alpha-amino groups of hemoglobin. Effect on functional properties.
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TLDR
These carboxymethylated hybrids may provide a useful model system for studies on the binding of anions to hemoglobin or on the interaction of CO2 with hemoglobin to form the carbamate Hb-NH-COO-.About:
This article is published in Journal of Biological Chemistry.The article was published on 1983-10-10 and is currently open access. It has received 48 citations till now. The article focuses on the topics: Cooperativity & Hemoglobin A.read more
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Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some Physiology Blut ist ein ganz besondrer Saft1
Patent
N-terminally chemically modified protein compositions and methods
TL;DR: In this article, methods and compositions relating to the attachment of water soluble polymers to proteins are presented. But they do not specify any methods for N-terminally modifying proteins or analogs thereof, and their resultant compositions, including novel Nterminally chemically modified GCSF compositions and related methods of preparation.
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Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions.
TL;DR: The pronounced sensitivity of the oxygen affinity ofbovine hemoglobin to chloride concentration and to pH suggests that in bovine species these are the modulators of oxygen transport in vivo.
Patent
Polymer conjugates of interferon beta-1a and their uses
TL;DR: An interferon beta polypeptide comprising inter-feron-beta 1a coupled to a polymer containing a polyalkylene glycol moiety was proposed in this paper.
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Subunit dissociations in natural and recombinant hemoglobins.
Lois R. Manning,W T Jenkins,J R Hess,Kim D. Vandegriff,Robert M. Winslow,James M. Manning,James M. Manning +6 more
TL;DR: A tetramer dissociation constant can now be determined readily and used together with other criteria for characterization of hemoglobins and their interaction with small regulatory molecules.
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Reductive alkylation of amino groups in proteins.
Gary E. Means,Robert E. Feeney +1 more
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Alkylation and identification of the histidine residues at the active site of ribonuclease.
TL;DR: The present communication is concerned with theracterization of the two products of the reaction, the establishment of the position of the amino acid residues altered in each instance, and the determination of which of theTwo structural isomers is formed when a given imidazole ring in ribonuclease is alkylated by iodoacetate.
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The Nature of the Amino Acid Residues Involved in the Inactivation of Ribonuclease by Iodoacetate
TL;DR: The fact, that the pH optimum for the reaction leading to the formation of imidazole carboxymethyl ribonuclease is around pH 5.5 to 6, instead of at the more alkaline pH values observed for the alkylation of cy-N-acetylhistidine, suggests that inactivation takes place as a result of substitution on a particular one of the four histidine residues present in rib onuclease.
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The interaction of 2,3-diphosphoglycerate with various human hemoglobins
TL;DR: Results suggest that the N-terminal amino groups of the non-α-chains are involved in the binding of 2,3-DPG to hemoglobin.