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The First Korean Family with Hemoglobin-M Milwaukee-2 Leading to Hereditary Methemoglobinemia.
Yonsei Med J
December 2020
Department of Pediatrics, Chonnam National University Hwasun Hospital, Hwasun, Korea.
Hemoglobin M (HbM) is a group of abnormal hemoglobin variants that form methemoglobin, which leads to cyanosis and hemolytic anemia. HbM-Milwaukee-2 is a rare variant caused by the point mutation CAC>TAC on codon 93 of the hemoglobin subunit beta () gene, resulting in the replacement of histidine by tyrosine. We here report the first Korean family with HbM-Milwaukee-2, whose diagnosis was confirmed by gene sequencing.
View Article and Find Full Text PDFHeterogeneity between Two α Subunits of αβ Human Hemoglobin and O Binding Properties: Raman, H Nuclear Magnetic Resonance, and Terahertz Spectra.
Biochemistry
November 2017
Research Center for Micro-Nano Technology, Hosei University, Koganei, Tokyo 184-0003, Japan.
Following a previous detailed investigation of the β subunit of αβ human adult hemoglobin (Hb A), this study focuses on the α subunit by using three natural valency hybrid α(Fe-deoxy/O)β(Fe) hemoglobin M (Hb M) in which O cannot bind to the β subunit: Hb M Hyde Park (β92His → Tyr), Hb M Saskatoon (β63His → Tyr), and Hb M Milwaukee (β67Val → Glu). In contrast with the β subunit that exhibited a clear correlation between O affinity and Fe-His stretching frequencies, the Fe-His stretching mode of the α subunit gave two Raman bands only in the T quaternary structure. This means the presence of two tertiary structures in α subunits of the αβ tetramer with T structure, and the two structures seemed to be nondynamical as judged from terahertz absorption spectra in the 5-30 cm region of Hb M Milwaukee, α(Fe-deoxy)β(Fe).
View Article and Find Full Text PDFHemoglobin M (Milwaukee) affects arterial oxygen saturation and makes pulse oximetry unreliable.
Anesthesiology
April 2006
Department of Anesthesiology, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy.
Biochemistry
July 2004
School of Health Sciences, Kanazawa University Faculty of Medicine, Kanazawa 920-0942, Japan.
The alpha-abnormal hemoglobin (Hb) M variants show physiological properties different from the beta-abnormal Hb M variants, that is, extremely low oxygen affinity of the normal subunit and extraordinary resistance to both enzymatic and chemical reduction of the abnormal met-subunit. To get insight into the contribution of heme structures to these differences among Hb M's, we examined the 406.7-nm excited resonance Raman (RR) spectra of five Hb M's in the frequency region from 1700 to 200 cm(-1).
View Article and Find Full Text PDFDNA sequence analysis proves Hb M-Milwaukee-2 is due to beta-globin gene codon 92 (CAC-->TAC), the presumed mutation of Hb M-Hyde Park and Hb M-Akita.
Hemoglobin
January 1998
Department of Pediatrics, Mayo Clinic, Rochester, MN 55905, USA.
Among the causes of congenital methemoglobinemia, Hb M-Milwaukee-2 was one of the earliest described, in a patient who also had Hb E trait. The structure of Hb M-Milwaukee-2 has been elusive. DNA sequence analysis, as here reported, proves that this hemoglobin variant is due to the mutation CAC-->TAC at codon 92 of the beta-globin gene, corresponding to the substitution of tyrosine for histidine.
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