Hemoglobin subunit alpha

HBA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1A00, 1A01, 1A0U, 1A0Z, 1A3N, 1A3O, 1A9W, 1ABW, 1ABY, 1AJ9, 1B86, 1BAB, 1BBB, 1BIJ, 1BUW, 1BZ0, 1BZ1, 1BZZ, 1C7B, 1C7C, 1C7D, 1CLS, 1CMY, 1COH, 1DKE, 1DXT, 1DXU, 1DXV, 1FDH, 1FN3, 1G9V, 1GBU, 1GBV, 1GLI, 1GZX, 1HAB, 1HAC, 1HBA, 1HBB, 1HBS, 1HCO, 1HDB, 1HGA, 1HGB, 1HGC, 1HHO, 1IRD, 1J3Y, 1J3Z, 1J40, 1J41, 1J7S, 1J7W, 1J7Y, 1JY7, 1K0Y, 1K1K, 1KD2, 1LFL, 1LFQ, 1LFT, 1LFV, 1LFY, 1LFZ, 1LJW, 1M9P, 1MKO, 1NEJ, 1NIH, 1NQP, 1O1I, 1O1J, 1O1K, 1O1L, 1O1M, 1O1N, 1O1O, 1O1P, 1QI8, 1QSH, 1QSI, 1QXD, 1QXE, 1R1X, 1R1Y, 1RPS, 1RQ3, 1RQ4, 1RQA, 1RVW, 1SDK, 1SDL, 1SHR, 1SI4, 1THB, 1UIW, 1VWT, 1XXT, 1XY0, 1XYE, 1XZ2, 1XZ4, 1XZ5, 1XZ7, 1XZU, 1XZV, 1Y01, 1Y09, 1Y0A, 1Y0C, 1Y0D, 1Y0T, 1Y0W, 1Y22, 1Y2Z, 1Y31, 1Y35, 1Y45, 1Y46, 1Y4B, 1Y4F, 1Y4G, 1Y4P, 1Y4Q, 1Y4R, 1Y4V, 1Y5F, 1Y5J, 1Y5K, 1Y7C, 1Y7D, 1Y7G, 1Y7Z, 1Y83, 1Y85, 1Y8W, 1YDZ, 1YE0, 1YE1, 1YE2, 1YEN, 1YEO, 1YEQ, 1YEU, 1YEV, 1YFF, 1YG5, 1YGD, 1YGF, 1YH9, 1YHE, 1YHR, 1YIE, 1YIH, 1YVQ, 1YVT, 1YZI, 1Z8U, 2D5Z, 2D60, 2DN1, 2DN2, 2DN3, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHD, 2HHE, 2M6Z, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HXN, 3IA3, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 3ODQ, 3ONZ, 3OO4, 3OO5, 3OVU, 3P5Q, 3QJB, 3QJC, 3QJD, 3QJE, 3R5I, 3S48, 3S65, 3S66, 3SZK, 3WCP, 3WHM, 4FC3, 4HHB, 4IJ2, 4L7Y, 4M4A, 4M4B, 4MQC, 4MQG, 4MQH, 4MQI, 4MQJ, 4MQK, 4N7N, 4N7O, 4N7P, 4N8T, 4NI0, 4NI1, 4ROL, 4ROM, 4WJG, 4X0L, 4XS0, 6HBW, 5E29, 5E6E, 5EE4, 5HU6, 5JDO, 5KDQ, 5E83,%%s1Y01, 1Z8U, 1BZ1
Identifiers
Aliases	HBA1, HBA-T3, HBH, hemoglobin subunit alpha 1, METHBA, ECYT7
External IDs	OMIM: 141800; MGI: 96015; HomoloGene: 469; GeneCards: HBA1; OMA:HBA1 - orthologs
Gene location (Human)
Chr.	Chromosome 16 (human)
End	177,522 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	32,234,465 bp
RNA expression pattern
	Top expressed in
	monocyte; ; blood; ; bone marrow; ; bone marrow cells; ; placenta; ; spleen; ; ganglionic eminence; ; muscle of thigh; ; olfactory zone of nasal mucosa; ; apex of heart;
	Top expressed in
	bone marrow; ; spleen; ; lung; ; yolk sac; ; neural tube; ; Mesencephalon; ; heart; ; cerebellar cortex; ; genital tubercle; ; zone of skin;
	More reference expression data
	n/a
Gene ontology
Molecular function	iron ion binding; oxygen binding; peroxidase activity; oxygen carrier activity; metal ion binding; protein binding; heme binding; haptoglobin binding; organic acid binding;
Cellular component	cytosol; endocytic vesicle lumen; blood microparticle; membrane; extracellular region; cytosolic small ribosomal subunit; hemoglobin complex; extracellular exosome; haptoglobin-hemoglobin complex; extracellular space;
Biological process	positive regulation of cell death; protein heterooligomerization; oxygen transport; receptor-mediated endocytosis; bicarbonate transport; hydrogen peroxide catabolic process; response to hydrogen peroxide; cellular oxidant detoxification; transport;
	Sources:Amigo / QuickGO
Orthologs
	3039
	15122
	ENSG00000206172
	ENSMUSG00000069919
	P69905
	Q91VB8
	NM_000558
	NM_008218
	NP_000508; NP_000508.1; NP_000549.1
	NP_001077424
	Wikidata
View/Edit Human	View/Edit Mouse

Hemoglobin subunit alpha, Hemoglobin, alpha 1,^[5] is a hemoglobin protein that in humans is encoded by the HBA1 gene.^[6]

Gene

The human alpha globin gene cluster located on chromosome 16 spans about 30 kb and includes seven loci: 5'- zeta - pseudozeta - mu - pseudoalpha-1 - alpha-2 - alpha-1 - theta - 3'. The alpha-2 (HBA2) and alpha-1 (HBA1; this gene) coding sequences are identical. These genes differ slightly over the 5' untranslated regions and the introns, but they differ significantly over the 3' untranslated regions.^[6]

Protein

Two alpha chains plus two beta chains constitute HbA, which in normal adult life accounts for about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with fetal hemoglobin (HbF), composed of alpha and gamma chains, make up the remaining 3% of adult hemoglobin.^[6]

Clinical significance

Alpha thalassemias result from deletions of each of the alpha genes as well as deletions of both HBA2 and HBA1; some nondeletion alpha thalassemias have also been reported.^[6]

Interactions

Hemoglobin subunit alpha has been shown to interact with hemoglobin subunit beta (HBB).^[7]^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000206172 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000069919 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "HBA1 gene: MedlinePlus Genetics".
^ ^a ^b ^c ^d "Entrez Gene: HBA1 hemoglobin, alpha 1".
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.957-68&rft.date=2005-09&rft_id=info:hdl/11858/00-001M-0000-0010-8592-0&rft_id=https://api.semanticscholar.org/CorpusID:8235923#id-name=S2CID&rft_id=info:pmid/16169070&rft_id=info:doi/10.1016/j.cell.2005.08.029&rft.aulast=Stelzl&rft.aufirst=U&rft.au=Worm, U&rft.au=Lalowski, M&rft.au=Haenig, C&rft.au=Brembeck, FH&rft.au=Goehler, H&rft.au=Stroedicke, M&rft.au=Zenkner, M&rft.au=Schoenherr, A&rft.au=Koeppen, S&rft.au=Timm, J&rft.au=Mintzlaff, S&rft.au=Abraham, C&rft.au=Bock, N&rft.au=Kietzmann, S&rft.au=Goedde, A&rft.au=Toksöz, E&rft.au=Droege, A&rft.au=Krobitsch, S&rft.au=Korn, B&rft.au=Birchmeier, W&rft.au=Lehrach, H&rft.au=Wanker, EE&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
^ Shaanan B (November 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. 171 (1): 31–59. doi:10.1016/S0022-2836(83)80313-1. PMID 6644819.31-59&rft.date=1983-11&rft_id=info:doi/10.1016/S0022-2836(83)80313-1&rft_id=info:pmid/6644819&rft.au=Shaanan B&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">

Turbpaiboon C, Svasti S, Sawangareetakul P, et al. (2002). "Hb Siam [alpha15(A13)Gly→Arg (alpha1) (GGT→CGT)] is a typical alpha chain hemoglobinopathy without an alpha-thalassemic effect". Hemoglobin. 26 (1): 77–81. doi:10.1081/HEM-120002944. PMID 11939517. S2CID 85035930.77-81&rft.date=2002&rft_id=https://api.semanticscholar.org/CorpusID:85035930#id-name=S2CID&rft_id=info:pmid/11939517&rft_id=info:doi/10.1081/HEM-120002944&rft.aulast=Turbpaiboon&rft.aufirst=C&rft.au=Svasti, S&rft.au=Sawangareetakul, P&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Yalçin A, Avcu F, Beyan C, et al. (1995). "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala→Glu]". Hemoglobin. 18 (6): 433–5. doi:10.3109/03630269409045775. PMID 7713747.433-5&rft.date=1995&rft_id=info:doi/10.3109/03630269409045775&rft_id=info:pmid/7713747&rft.aulast=Yalçin&rft.aufirst=A&rft.au=Avcu, F&rft.au=Beyan, C&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Giardina B, Messana I, Scatena R, Castagnola M (1995). "The multiple functions of hemoglobin". Crit. Rev. Biochem. Mol. Biol. 30 (3): 165–96. doi:10.3109/10409239509085142. PMID 7555018.165-96&rft.date=1995&rft_id=info:doi/10.3109/10409239509085142&rft_id=info:pmid/7555018&rft.aulast=Giardina&rft.aufirst=B&rft.au=Messana, I&rft.au=Scatena, R&rft.au=Castagnola, M&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Higgs DR, Vickers MA, Wilkie AO, et al. (1989). "A review of the molecular genetics of the human alpha-globin gene cluster". Blood. 73 (5): 1081–104. doi:10.1182/blood.V73.5.1081.1081. PMID 2649166.1081-104&rft.date=1989&rft_id=info:doi/10.1182/blood.V73.5.1081.1081&rft_id=info:pmid/2649166&rft.aulast=Higgs&rft.aufirst=DR&rft.au=Vickers, MA&rft.au=Wilkie, AO&rft_id=https://doi.org/10.1182%2Fblood.V73.5.1081.1081&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Schillirò G, Russo-Mancuso G, Dibenedetto SP, et al. (1992). "Six rare hemoglobin variants found in Sicily". Hemoglobin. 15 (5): 431–7. doi:10.3109/03630269108998862. PMID 1802885.431-7&rft.date=1992&rft_id=info:doi/10.3109/03630269108998862&rft_id=info:pmid/1802885&rft.aulast=Schillirò&rft.aufirst=G&rft.au=Russo-Mancuso, G&rft.au=Dibenedetto, SP&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Vafa M, Troye-Blomberg M, Anchang J, et al. (2008). "Multiplicity of Plasmodium falciparum infection in asymptomatic children in Senegal: relation to transmission, age and erythrocyte variants". Malar. J. 7: 17. doi:10.1186/1475-2875-7-17. PMC 2267475. PMID 18215251.
Datta P, Chakrabarty S, Chakrabarty A, Chakrabarti A (2008). "Membrane interactions of hemoglobin variants, HbA, HbE, HbF and globin subunits of HbA: effects of aminophospholipids and cholesterol". Biochim. Biophys. Acta. 1778 (1): 1–9. doi:10.1016/j.bbamem.2007.08.019. PMID 17916326.1-9&rft.date=2008&rft_id=info:doi/10.1016/j.bbamem.2007.08.019&rft_id=info:pmid/17916326&rft.aulast=Datta&rft.aufirst=P&rft.au=Chakrabarty, S&rft.au=Chakrabarty, A&rft.au=Chakrabarti, A&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Taylor JG, Ackah D, Cobb C, et al. (2008). "Mutations and polymorphisms in hemoglobin genes and the risk of pulmonary hypertension and death in sickle cell disease". Am. J. Hematol. 83 (1): 6–14. doi:10.1002/ajh.21035. PMC 3509176. PMID 17724704.6-14&rft.date=2008&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509176#id-name=PMC&rft_id=info:pmid/17724704&rft_id=info:doi/10.1002/ajh.21035&rft.aulast=Taylor&rft.aufirst=JG&rft.au=Ackah, D&rft.au=Cobb, C&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509176&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Sahu SC, Simplaceanu V, Gong Q, et al. (2007). "Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector". Biochemistry. 46 (35): 9973–80. doi:10.1021/bi700935z. PMC 2532491. PMID 17691822.9973-80&rft.date=2007&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2532491#id-name=PMC&rft_id=info:pmid/17691822&rft_id=info:doi/10.1021/bi700935z&rft.aulast=Sahu&rft.aufirst=SC&rft.au=Simplaceanu, V&rft.au=Gong, Q&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2532491&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Sorour Y, Heppinstall S, Porter N, et al. (2007). "Is routine molecular screening for common alpha-thalassaemia deletions necessary as part of an antenatal screening programme?". Journal of Medical Screening. 14 (2): 60–1. doi:10.1258/096914107781261981. PMID 17626702. S2CID 24823660.60-1&rft.date=2007&rft_id=https://api.semanticscholar.org/CorpusID:24823660#id-name=S2CID&rft_id=info:pmid/17626702&rft_id=info:doi/10.1258/096914107781261981&rft.aulast=Sorour&rft.aufirst=Y&rft.au=Heppinstall, S&rft.au=Porter, N&rft_id=https://doi.org/10.1258%2F096914107781261981&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Hung CC, Lee CN, Chen CP, et al. (2007). "Molecular assay of -alpha(3.7) and -alpha(4.2) deletions causing alpha-thalassemia by denaturing high-performance liquid chromatography". Clin. Biochem. 40 (11): 817–21. doi:10.1016/j.clinbiochem.2007.03.018. PMID 17512924.817-21&rft.date=2007&rft_id=info:doi/10.1016/j.clinbiochem.2007.03.018&rft_id=info:pmid/17512924&rft.aulast=Hung&rft.aufirst=CC&rft.au=Lee, CN&rft.au=Chen, CP&rft_id=http://ntur.lib.ntu.edu.tw//handle/246246/132682&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Ye BC, Zhang Z, Lei Z (2007). "Molecular analysis of alpha/beta-thalassemia in a southern Chinese population". Genet. Test. 11 (1): 75–83. doi:10.1089/gte.2006.0502. PMID 17394396.75-83&rft.date=2007&rft_id=info:doi/10.1089/gte.2006.0502&rft_id=info:pmid/17394396&rft.aulast=Ye&rft.aufirst=BC&rft.au=Zhang, Z&rft.au=Lei, Z&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Dilley J, Ganesan A, Deepa R, et al. (2007). "Association of A1C with cardiovascular disease and metabolic syndrome in Asian Indians with normal glucose tolerance". Diabetes Care. 30 (6): 1527–32. doi:10.2337/dc06-2414. PMID 17351274.1527-32&rft.date=2007&rft_id=info:doi/10.2337/dc06-2414&rft_id=info:pmid/17351274&rft.aulast=Dilley&rft.aufirst=J&rft.au=Ganesan, A&rft.au=Deepa, R&rft_id=https://doi.org/10.2337%2Fdc06-2414&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Fonseka PV, Vasudevan G, Clarizia LJ, McDonald MJ (2007). "Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly". Protein J. 26 (4): 257–63. doi:10.1007/s10930-006-9067-7. PMID 17191128. S2CID 24601675.257-63&rft.date=2007&rft_id=https://api.semanticscholar.org/CorpusID:24601675#id-name=S2CID&rft_id=info:pmid/17191128&rft_id=info:doi/10.1007/s10930-006-9067-7&rft.aulast=Fonseka&rft.aufirst=PV&rft.au=Vasudevan, G&rft.au=Clarizia, LJ&rft.au=McDonald, MJ&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
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Hussein OA, Gefen Y, Zidan JM, et al. (2007). "LDL oxidation is associated with increased blood hemoglobin A1c levels in diabetic patients". Clin. Chim. Acta. 377 (1–2): 114–8. doi:10.1016/j.cca.2006.09.002. PMID 17070510.1–2&rft.pages=114-8&rft.date=2007&rft_id=info:doi/10.1016/j.cca.2006.09.002&rft_id=info:pmid/17070510&rft.aulast=Hussein&rft.aufirst=OA&rft.au=Gefen, Y&rft.au=Zidan, JM&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Pan W, Galkin O, Filobelo L, et al. (2007). "Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin". Biophys. J. 92 (1): 267–77. Bibcode:2007BpJ....92..267P. doi:10.1529/biophysj.106.094854. PMC 1697867. PMID 17040989.267-77&rft.date=2007&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1697867#id-name=PMC&rft_id=info:pmid/17040989&rft_id=info:doi/10.1529/biophysj.106.094854&rft_id=info:bibcode/2007BpJ....92..267P&rft.aulast=Pan&rft.aufirst=W&rft.au=Galkin, O&rft.au=Filobelo, L&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1697867&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Pistrosch F, Koehler C, Wildbrett J, Hanefeld M (2006). "Relationship between diurnal glucose levels and HbA1c in type 2 diabetes". Horm. Metab. Res. 38 (7): 455–9. doi:10.1055/s-2006-947838. PMID 16933182. S2CID 260166156.455-9&rft.date=2006&rft_id=https://api.semanticscholar.org/CorpusID:260166156#id-name=S2CID&rft_id=info:pmid/16933182&rft_id=info:doi/10.1055/s-2006-947838&rft.aulast=Pistrosch&rft.aufirst=F&rft.au=Koehler, C&rft.au=Wildbrett, J&rft.au=Hanefeld, M&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">
Chong YM, Tan JA, Zubaidah Z, et al. (2006). "Screening of concurrent alpha-thalassaemia 1 in beta-thalassaemia carriers". Med. J. Malaysia. 61 (2): 217–20. PMID 16898315.217-20&rft.date=2006&rft_id=info:pmid/16898315&rft.aulast=Chong&rft.aufirst=YM&rft.au=Tan, JA&rft.au=Zubaidah, Z&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">

External links

GeneReviews/NCBI/NIH/UW entry on Alpha-Thalassemia
OMIM entries on Alpha-Thalassemia
Overview of all the structural information available in the PDB for UniProt: P69905 (Hemoglobin subunit alpha) at the PDBe-KB.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000206172 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000069919 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] "HBA1 gene: MedlinePlus Genetics".

[entrez-6] "Entrez Gene: HBA1 hemoglobin, alpha 1".

[pmid16169070-7] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.957-68&rft.date=2005-09&rft_id=info:hdl/11858/00-001M-0000-0010-8592-0&rft_id=https://api.semanticscholar.org/CorpusID:8235923#id-name=S2CID&rft_id=info:pmid/16169070&rft_id=info:doi/10.1016/j.cell.2005.08.029&rft.aulast=Stelzl&rft.aufirst=U&rft.au=Worm, U&rft.au=Lalowski, M&rft.au=Haenig, C&rft.au=Brembeck, FH&rft.au=Goehler, H&rft.au=Stroedicke, M&rft.au=Zenkner, M&rft.au=Schoenherr, A&rft.au=Koeppen, S&rft.au=Timm, J&rft.au=Mintzlaff, S&rft.au=Abraham, C&rft.au=Bock, N&rft.au=Kietzmann, S&rft.au=Goedde, A&rft.au=Toksöz, E&rft.au=Droege, A&rft.au=Krobitsch, S&rft.au=Korn, B&rft.au=Birchmeier, W&rft.au=Lehrach, H&rft.au=Wanker, EE&rfr_id=info:sid/en.wikipedia.org:Hemoglobin subunit alpha" class="Z3988">

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