A variant hemoglobin assicated with α-Thalassemia-2

Moo-Penn, Winston F.; Baine, Rosalie M.; Jue, Danny L.; Johnson, Mary; McGuffey, James E.; Benson, Jane M.

doi:10.1016/0167-4838(83)90122-x

Cited by 31 publications

(3 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Other variants were produced in reticulocytes at a normal proportion as expected for an a chain variant (47)(48)(49)(50).…”

Section: "Byperunstable" Hbsmentioning

confidence: 93%

Unstable Hemoglobins

Ohba

1990

Hemoglobin

View full text Add to dashboard Cite

About 70 variants of Hb A with associated hemolytic disorders have been reported during the past 30 years. I have classified them according to four grades of severity of chronic hemolysis. Acute episodes of severe hemolysis may be seen in all classes. In addition, some 80 variants without overt hemolysis have given positive results with in vitro hemoglobin instability tests. The stereochemical bases for instability can be conjectured in most cases, although few unstable hemoglobins have actually been studied by X-ray crystallography. The mechanisms for denaturation of normal Hb A and its acceleration in unstable hemoglobins were proposed some 15 years ago. The alterations of membrane lipids and proteins leading to red cell senescence and the relevance of hemoglobin denaturation to this process are presently being investigated. Several "hyperunstable" variants are clinically silent, or equivalent to a thalassemia, probably because of very efficient degradation of the abnormal chains.

show abstract

“…Other variants were produced in reticulocytes at a normal proportion as expected for an a chain variant (47)(48)(49)(50).…”

Section: "Byperunstable" Hbsmentioning

confidence: 93%

Unstable Hemoglobins

Ohba

1990

Hemoglobin

View full text Add to dashboard Cite

show abstract

“…Two other missense mutations have been described at this position of the α-globin, namely Hb Evanston (HBA1, Trp14Arg) (10,11), and Hb Bladensburg (HBA2, Trp14Cys; M. Gallivan, personal communication, 2007). Hb Evanston was found alone and in the presence of common α-thal deletions in three independent Asian cases.…”

mentioning

confidence: 96%

A New Stable α Chain Variant: Hb Basel [α14(A12)Trp→Leu (α1)]

Hergersberg¹,

Brunner-Agten²,

Kühne³

et al. 2010

Hemoglobin

View full text Add to dashboard Cite

We describe a heterozygosity for a new missense mutation on the alpha1-globin gene of an 18-year-old woman of Portuguese ancestry with severe hypochromic anemia and iron deficiency. Hemoglobin (Hb) analysis by high performance liquid chromatography (HPLC) found a prominent peak constituting about 12% of total Hb. Sequencing of the globin genes of the index patient found the mutation alpha14(A12)Trp-->Leu (alpha1), HBA1:c.44G

show abstract

“…Peptide maps were prepared by chromatography in a solvent of isoamyl alcohol /pyridine/water (7:7:6 v/v), and electrophoresis was done at pH 6.4 for 150 min at 28 V/cm (Bennett, 1967). Peptides resolved by ion-exchange column chromatography and by reverse-phase HPLC (Jones, 1970;Moo-Penn et al, 1983) were hydrolyzed in 6 N HC1 at 110 °C for 24 h in vacuo, and the amino acid compositions were determined by using a Beckman 121 amino acid analyzer. Sequence data were obtained from a Beckman 890C sequencer (program 121078) with treatment of the spinning cup with polybrene.…”

mentioning

confidence: 99%

Hemoglobin Brockton [.beta.138 (H16) Ala .fwdarw. Pro]: an unstable variant near the C-terminus of the .beta.-subunits with normal oxygen-binding properties

Moo-Penn

Jue²,

Johnson³

et al. 1988

Biochemistry

Self Cite

View full text Add to dashboard Cite

Hemoglobin Brockton [beta 138 (H16) Ala----Pro] is an unstable variant associated with a mild anemia. It has the same electrophoretic mobility as and cannot be resolved from Hb A. Oxygen affinity measurements of blood and hemolysate do not indicate biphasic oxygen saturation, showing that the functional properties of the variant are very similar to those of Hb A. This implies that the introduction of proline into the H-helix at position 138 does not disrupt the critical inter- and intrasubunit hydrogen bonds and salt bridges at the beta carboxyl-terminal dipeptide, since these polar interactions are essential for the normal oxygen-binding properties of hemoglobin. X-ray crystallographic data are consistent with these findings and show that the consequences of the beta 138 Ala----Pro substitution are almost entirely confined to the immediate vicinity of the mutation site. Instability probably results from the inability of a buried hydrogen bond to form between Pro 138 beta and Val 134 beta.

show abstract

A variant hemoglobin assicated with α-Thalassemia-2

Cited by 31 publications

References 21 publications

Unstable Hemoglobins

Unstable Hemoglobins

A New Stable α Chain Variant: Hb Basel [α14(A12)Trp→Leu (α1)]

Hemoglobin Brockton [.beta.138 (H16) Ala .fwdarw. Pro]: an unstable variant near the C-terminus of the .beta.-subunits with normal oxygen-binding properties

Contact Info

Product

Resources

About