A New Hemoglobin Variant Found During Hb A1cMeasurement: Hb Hokusetsu [β52(D3)Asp→Gly]
| ISSN: | 1532-432X 0363-0269 |
|---|---|
| DOI: | 10.3109/03630269809071530 |
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aac29baac7b8d318d50a1d427be42648 https://doi.org/10.3109/03630269809071530 |
| Přírůstkové číslo: | edsair.doi.dedup.....aac29baac7b8d318d50a1d427be42648 |
| Autor: | T Tsubakio, O Kishida, Akira Shimizu, Ayako Miyazaki, S Sumi, Kiyohiro Imai, M Kishikawa, Toyofumi Nakanishi |
| Rok vydání: | 1998 |
| Předmět: |
Male
Hemoglobins Abnormal Electrospray ionization Molecular Sequence Data Clinical Biochemistry Peptide High-performance liquid chromatography Lysyl endopeptidase Diabetes Mellitus medicine Humans Selected ion monitoring Amino Acid Sequence Globin Chromatography High Pressure Liquid Genetics (clinical) chemistry.chemical_classification Chromatography Chemistry Biochemistry (medical) Hemoglobin variants Hematology Middle Aged Trypsin Molecular biology medicine.drug |
| Zdroj: | Hemoglobin. 22:355-371 |
| ISSN: | 1532-432X 0363-0269 |
| DOI: | 10.3109/03630269809071530 |
| Popis: | A new beta chain variant was accidentally found through the assay of Hb A1c in a diabetic patient. The variant was detected by polyacrylamide gel isoelectrofocusing and electrospray ionization mass spectrometry. For sequence determination, globin was cleaved with combination of trypsin and lysyl endopeptidase and analyzed by high performance liquid chromatography connected to electrospray ionization mass spectrometry. An abnormal betaT-5 peptide was found by reconstructed selected ion monitoring. The collision-induced dissociation spectrum of an ion derived from the abnormal betaT-5 peptide revealed a new substitution, [beta52(D3)Asp-->Gly], named Hb Hokusetsu. The sequence was confirmed with an automatic sequencer using peptides isolated by reversed phase high performance liquid chromatography. Amplification of the beta-globin exon 2 and nucleotide sequencing revealed a GAT-->GGT mutation in codon 52 corresponding to an Asp-->Gly replacement. Electrospray ionization mass spectrometry analysis of the hemolysate showed a reasonable value of 10.4% for glycated globin. The variant migrated as Hb S on isoelectrofocusing. Hematological analysis revealed normal parameters. The patient's hemolysate showed normal stability in the isopropanol test. Oxygen equilibrium studies on the patient's red blood cells and hemolysate showed no significant change in oxygen affinity or cooperativity. |
| Databáze: | OpenAIRE |
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