Globin


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globin

[′glō·bən]
(biochemistry)
Any of a class of soluble histone proteins obtained from animal hemoglobins.

Globin

 

the albuminous part of the complex protein hemoglobin, which includes four globin chains. Up to 30 percent of the proteinaceous nitrogen of globin is found in the diamino acids (arginine, lysine, and histidine). This is also characteristic of the histones; however, in contrast to the latter, globin contains little tyrosine. The isoelectric point of globin is 7.5; it is readily soluble in water but is precipitated by alcohol or acetone. The bond between heme and globin is stable and broken only in an acidic environment. After detachment of the heme, the protein loses its native properties. The rate of synthesis of globin in the body is very high, owing to the frequent replacement of the erythrocytes. The synthesis of globin takes place at the sites where the erythrocytes are formed; in animals having nucleated erythrocytes, globin synthesis may be observed directly in the erythrocytes of the blood. Genetically induced anomalies in globin synthesis determine some “molecular” blood diseases, such as sickle-cell anemia and Mediterranean anemia. In some cases the difference of anomalous globin consists in the replacement of just one amino acid in the polypeptide chain.

A. A. BOLDYREV

References in periodicals archive ?
This is due to increased synthesis of I3-globin (G) chains, thereby reducing imbalance between alpha and non-alpha globin chains and resulting in decreased disease severity.
Results showed that polymorphism exists in 2 out of 206 screened [beta]-thalassemia patients and amplified region of their gamma beta globin gene displayed multiple banding patterns after overnight restriction digestion.
As the controls, the original construct of EGFPd2 without the beta globin UTRs under the control of T7 promoter were used.
The only globin chain sequence reported from Viper snakes is from Vipera aspis describing the sequence of [alpha]-chain of hemoglobin (Duguet et al., 1974).
Subsequent beta globin sequencing revealed a heterozygous beta-plus thalassemia mutation, while analysis for alpha globin deletions revealed a heterozygous Southeast Asian (SEA) two-gene deletion, consistent with--/[alpha][alpha] alpha thalassemia minor.
Constituent globin chains separation and quantitation were carried out by electrophoresis on 12% polyacrylamide gels containing 6M urea and 2% Triton X-100 in 5% acetic acid (AUT-PAGE) [14] and reversed-phase high-performance liquid chromatography (RP-HPLC).
[4] The [[beta].sup.E] gene results in inefficient synthesis, as borne out by studies that show decreased [[beta].sup.E] globin chain synthesis, [5] and there is also evidence that the [[beta].sup.E] messenger RNA is relatively unstable.
This enlargement is due to damages to the membrane of RBC (red blood cells) by the excessive a globin, resulting severe anemia and in response, body begin to increase the production of RBC, resulting expansion of the bone marrow up to 15-30 times the normal amount.
Consumer tests have demonstrated that cooked hams prepared with the globin protein isolated with MaxiPro HSP were preferred in taste over hams prepared with pure plasma protein, or with traditionally decoloured globin protein.
They propose that individual globin chains might have functional roles in these cells and Hb might be involved in pathologies associated with respiratory diseases.
It is expected that the pharmacological induction of HbF can correct the globin chain imbalance in [beta]-thalassemia patients, while inhibit HbS polymerization in SCD patients [28-32].
The alpha globin variant Constant Spring chains also form tetramers with [beta]-globin chains, creating hemoglobin Constant Spring, thereby reducing the number of free [beta]-globin chains available to form [beta]-globin tetramers of HbH.