1. 1,3-Biphosphoglycerate
2. 1,3-Biphosphoglyceric acid
3. 1,3-Bisphosphoglycerate
4. 1,3-Diphosphoglycerate
5. 1,3-bis-phosphoglycerate
6. 1,3-diphosphateglycerate
7. 13-DPG
8. 2-hydroxy-3-(phosphonooxy)-Propanoic acid 1-anhydride with phosphorate
9. 2-hydroxy-3-(phosphonooxy)-Propanoic acid 1-anhydride with phosphoric acid
10. 3-P-glyceroyl-P
11. 3-Phosphoglyceroyl phosphate
12. 3-phospho-D-glyceroyl-phosphate
13. 3-Phospho-D-glyceroyl phosphate
14. 3-phosphoglyceroyl-P
15. 3-phosphoglyceroyl-phosphate
16. DPG
17. Glycerate 1,3-Biphosphate
18. Glyceric acid 1,3-biphosphate
19. Glyceric acid 1,3-biphosphic acid
20. P-glyceroyl-P
21. Phosphoglyceroyl-P
22. glycerate 1,3-bisphosphate
23. glycerate 1,3-diphosphate
24. 2-hydroxy-3-(phosphonooxy)-Propanoate
25. 2-hydroxy-3-(phosphonooxy)-Propanoic acid

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• Cytoplasm

• Blood
• Cellular Cytoplasm

1. Inoue H, Moriyasu M, Hamasaki N: Metabolism of 3-phosphoglyceroyl phosphate in phosphoenolpyruvate-enriched human erythrocytes. J Biol Chem. 1987 Jun 5;262(16):7635-8. [PubMed ]
2. Fabry ME, Nagel RL: Heterogeneity of red cells in the sickler: a characteristic with practical clinical and pathophysiological implications. Blood Cells. 1982;8(1):9-15. [PubMed ]
3. Flachner B, Varga A, Szabo J, Barna L, Hajdu I, Gyimesi G, Zavodszky P, Vas M: Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase. Biochemistry. 2005 Dec 27;44(51):16853-65. [PubMed ]
4. Carreras J, Bartrons R, Climent F, Cusso R: Bisphosphorylated metabolites of glycerate, glucose, and fructose: functions, metabolism and molecular pathology. Clin Biochem. 1986 Dec;19(6):348-58. [PubMed ]
5. Fujii H: [Red cell glycolytic intermediates] Nippon Rinsho. 1995 Mar;53 Su Pt 2:234-8. [PubMed ]
6. Sayed A, Matsuyama S, Inoue K, Alsina J, Cai F, Chen J, Inouye M: ATPase and GTPase activities copurifying with GTP-binding proteins in E. coli. J Mol Microbiol Biotechnol. 2000 Jul;2(3):261-3. [PubMed ]
7. Fokina KV, Dainyak MB, Nagradova NK, Muronetz VI: A study on the complexes between human erythrocyte enzymes participating in the conversions of 1,3-diphosphoglycerate. Arch Biochem Biophys. 1997 Sep 15;345(2):185-92. [PubMed ]
8. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed ]
9. Jovanovic S, Du Q, Crawford RM, Budas GR, Stagljar I, Jovanovic A: Glyceraldehyde 3-phosphate dehydrogenase serves as an accessory protein of the cardiac sarcolemmal K(ATP) channel. EMBO Rep. 2005 Sep;6(9):848-52. [PubMed ]
10. Oimomi M, Yoshimura Y, Kubota S, Tanke G, Takagi K, Baba S: Effect of hydrocortisone on the synthesis of 2,3-diphosphoglycerate in human erythrocytes. Transfusion. 1982 Jul-Aug;22(4):266-8. [PubMed ]
11. Joao HC, Williams RJ: The anatomy of a kinase and the control of phosphate transfer. Eur J Biochem. 1993 Aug 15;216(1):1-18. [PubMed ]
12. Wikipedia

1. Bisphosphoglycerate mutase
2. Acylphosphatase-1
3. Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
4. Phosphoglycerate kinase 1

1. 2,3-bisphosphoglycerate mutase, erythrocyte
2. 2,3-bisphosphoglycerate synthase
3. BPGM
4. BPG-dependent PGAM

MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVL
NRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYN
VTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRG
KTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEA
IQAAIKKVEDQGKVKQAKK

• Gluconeogenesis (map00010 )

• 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate

• PGAM (PF00300 )

• None

• None

ATGTCCAAGTACAAACTTATTATGTTAAGACATGGAGAGGGTGCTTGGAATAAGGAGAAC
CGTTTTTGTAGCTGGGTGGATCAGAAACTCAACAGCGAAGGAATGGAGGAAGCTCGGAAC
TGTGGGAAGCAACTCAAAGCGTTAAACTTTGAGTTTGATCTTGTATTCACATCTGTCCTT
AATCGGTCCATTCACACAGCCTGGCTGATCCTGGAAGAGCTAGGCCAGGAATGGGTGCCT
GTGGAAAGCTCCTGGCGTCTAAATGAGCGTCACTATGGGGCCTTGATCGGTCTCAACAGG
GAGCAGATGGCTTTGAATCATGGTGAAGAACAAGTGAGGCTCTGGAGAAGAAGCTACAAT
GTAACCCCGCCTCCCATTGAGGAGTCTCATCCTTACTACCAAGAAATCTACAACGACCGG
AGGTATAAAGTATGCGATGTGCCCTTGGATCAACTGCCACGGTCGGAAAGCTTAAAGGAT
GTTCTGGAGAGACTCCTTCCCTATTGGAATGAAAGGATTGCTCCCGAAGTATTACGTGGC
AAAACCATTCTGATATCTGCTCATGGAAATAGCAGTAGGGCACTCCTAAAACACCTGGAA
GGTATCTCAGATGAAGACATCATCAACATTACTCTTCCTACTGGAGTCCCCATTCTTCTG
GAATTGGATGAAAACCTGCGTGCTGTTGGGCCTCATCAGTTCCTGGGTGACCAAGAGGCG
ATCCAAGCAGCCATTAAGAAAGTAGAAGATCAAGGAAAAGTGAAACAAGCTAAAAAATAG

1. Joulin V, Peduzzi J, Romeo PH, Rosa R, Valentin C, Dubart A, Lapeyre B, Blouquit Y, Garel MC, Goossens M, et al.: Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. EMBO J. 1986 Sep;5(9):2275-83. [PubMed ]
2. Cohen-Solal M, Joulin V, Romeo PH, Rosa R, Valentin C, Garel MC, Rosa J: Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence. Biomed Biochim Acta. 1987;46(2-3):S126-30. [PubMed ]
3. Joulin V, Garel MC, Le Boulch P, Valentin C, Rosa R, Rosa J, Cohen-Solal M: Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene. J Biol Chem. 1988 Oct 25;263(30):15785-90. [PubMed ]
4. Stafforini DM, Rollins EN, Prescott SM, McIntyre TM: The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties. J Biol Chem. 1993 Feb 25;268(6):3857-65. [PubMed ]
5. Craescu CT, Schaad O, Garel MC, Rosa R, Edelstein S: Structural modeling of the human erythrocyte bisphosphoglycerate mutase. Biochimie. 1992 Jun;74(6):519-26. [PubMed ]

1. Acylphosphate phosphohydrolase 1
2. Acylphosphatase, organ-common type isozyme
3. Acylphosphatase, erythrocyte isozyme

MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK

• Benzoate Degradation via CoA Ligation (map00632 )
• Gluconeogenesis (map00010 )
• Pyruvate Metabolism (map00620 )

• An acylphosphate + H2O = a carboxylate + phosphate

• Acylphosphatase (PF00708 )

• None

• None

ATGGCAGAGGGAAACACCCTGATATCAGTGGATTATGAAATTTTTGGGAAGGTGCAAGGG
GTGTTTTTCCGTAAGCATACTCAGGCTGAGGGTAAAAAGCTGGGATTGGTAGGCTGGGTC
CAGAACACTGACCGGGGCACAGTGCAAGGACAATTGCAAGGTCCAATCTCCAAGGTGCGT
CATATGCAGGAATGGCTTGAAACAAGAGGAAGTCCTAAATCACACATCGACAAAGCAAAC
TTCAACAATGAAAAAGTCATCTTGAAGTTGGATTACTCAGACTTCCAAATTGTAAAATAA

1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
2. Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G: A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. Biochemistry. 1986 Dec 2;25(24):8089-94. [PubMed ]
3. Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. FEBS Lett. 1995 Jun 26;367(2):145-8. [PubMed ]

1. Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
2. Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
3. GAPDH-2

MSKRDIVLTNVTVVQLLRQPCPVTRAPPPPEPKAEVEPQPQPEPTPVREEIKPPPPPLPP
HPATPPPKMVSVARELTVGINGFGRIGRLVLRACMEKGVKVVAVNDPFIDPEYMVYMFKY
DSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAAS
DHISAGAQRVVISAPSPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKVIHERF
GIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKL
TGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLG
DTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRDK

• Gluconeogenesis (map00010 )

• D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

• Gp_dh_C (PF02800 )
• Gp_dh_N (PF00044 )

• None

• None

ATGTCGAAGCGCGACATCGTCCTCACCAATGTCACCGTTGTCCAGTTGCTGCGACAGCCG
TGCCCGGTGACCAGAGCACCGCCCCCACCTGAGCCTAAGGCTGAAGTAGAGCCCCAGCCA
CAACCAGAGCCCACACCAGTCAGGGAGGAAATAAAGCCACCACCGCCACCACTGCCTCCT
CACCCCGCTACTCCTCCTCCTAAGATGGTGTCTGTGGCCCGGGAGCTGACTGTGGGCATC
AATGGATTTGGACGCATCGGTCGCCTGGTCCTGCGCGCCTGCATGGAGAAGGGTGTTAAG
GTGGTGGCTGTGAATGATCCATTCATTGACCCGGAATACATGGTGTACATGTTTAAGTAT
GACTCCACCCACGGCCGATACAAGGGAAGTGTGGAATTCAGGAATGGACAACTGGTCGTG
GACAACCATGAGATCTCTGTCTACCAGTGCAAAGAGCCCAAACAGATCCCCTGGAGGGCT
GTCGGGAGCCCCTACGTGGTGGAGTCCACAGGCGTGTACCTCTCCATACAGGCAGCTTCG
GACCACATCTCTGCAGGTGCTCAACGTGTGGTCATCTCCGCGCCCTCACCGGATGCACCA
ATGTTCGTCATGGGTGTCAATGAAAATGACTATAACCCTGGCTCCATGAACATTGTGAGC
AACGCGTCCTGCACCACCAACTGTTTGGCTCCCCTCGCCAAAGTCATCCACGAGCGATTT
GGGATCGTGGAAGGGTTGATGACCACAGTCCATTCCTACACGGCCACCCAGAAGACAGTG
GACGGGCCATCAAGGAAGGCCTGGCGAGATGGGCGGGGTGCCCACCAGAACATCATCCCA
GCCTCCACTGGGGCTGCGAAAGCTGTGACCAAAGTCATCCCAGAGCTCAAAGGGAAGCTG
ACAGGGATGGCGTTCCGGGTACCAACCCCGGATGTGTCTGTCGTGGACCTGACCTGCCGC
CTCGCCCAGCCTGCCCCCTACTCAGCCATCAAGGAGGCTGTAAAAGCAGCAGCCAAGGGG
CCCATGGCTGGCATCCTTGCCTACACCGAGGATGAGGTCGTCTCTACGGACTTCCTCGGT
GATACCCACTCGTCCATCTTCGATGCTAAGGCCGGCATTGCGCTCAATGACAATTTCGTG
AAGCTCATTTCATGGTACGACAACGAATATGGCTACAGTCACCGGGTGGTCGACCTCCTC
CGCTACATGTTCAGCCGAGACAAGTGA

1. Welch JE, Brown PL, O'Brien DA, Magyar PL, Bunch DO, Mori C, Eddy EM: Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J Androl. 2000 Mar-Apr;21(2):328-38. [PubMed ]

1. Primer recognition protein 2
2. PRP 2
3. Cell migration-inducing gene 10 protein

MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVL
MSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLE
NLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVN
LPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGM
AFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQ
ATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVV
KATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI

• Carbon fixation (map00710 )
• Gluconeogenesis (map00010 )

• ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate

• PGK (PF00162 )

• None

• None

ATGTCGCTTTCTAACAAGCTGACGCTGGACAAGCTGGACGTTAAAGGGAAGCGGGTCGTT
ATGAGAGTCGACTTCAATGTTCCTATGAAGAACAACCAGATAACAAACAACCAGAGGATT
AAGGCTGCTGTCCCAAGCATCAAATTCTGCTTGGACAATGGAGCCAAGTCGGTAGTCCTT
ATGAGCCACCTAGGCCGGCCTGATGGTGTGCCCATGCCTGACAAGTACTCCTTAGAGCCA
GTTGCTGTAGAACTCAAATCTCTGCTGGGCAAGGATGTTCTGTTCTTGAAGGACTGTGTA
GGCCCAGAAGTGGAGAAAGCCTGTGCCAACCCAGCTGCTGGGTCTGTCATCCTGCTGGAG
AACCTCCGCTTTCATGTGGAGGAAGAAGGGAAGGGAAAAGATGCTTCTGGGAACAAGGTT
AAAGCCGAGCCAGCCAAAATAGAAGCTTTCCGAGCTTCACTTTCCAAGCTAGGGGATGTC
TATGTCAATGATGCTTTTGGCACTGCTCACAGAGCCCACAGCTCCATGGTAGGAGTCAAT
CTGCCACAGAAGGCTGGTGGGTTTTTGATGAAGAAGGAGCTGAACTACTTTGCAAAGGCC
TTGGAGAGCCCAGAGCGACCCTTCCTGGCCATCCTGGGCGGAGCTAAAGTTGCAGACAAG
ATCCAGCTCATCAATAATATGCTGGACAAAGTCAATGAGATGATTATTGGTGGTGGAATG
GCTTTTACCTTCCTTAAGGTGCTCAACAACATGGAGATTGGCACTTCTCTGTTTGATGAA
GAGGGAGCCAAGATTGTCAAAGACCTAATGTCCAAAGCTGAGAAGAATGGTGTGAAGATT
ACCTTGCCTGTTGACTTTGTCACTGCTGACAAGTTTGATGAGAATGCCAAGACTGGCCAA
GCCACTGTGGCTTCTGGCATACCTGCTGGCTGGATGGGCTTGGACTGTGGTCCTGAAAGC
AGCAAGAAGTATGCTGAGGCTGTCACTCGGGCTAAGCAGATTGTGTGGAATGGTCCTGTG
GGGGTATTTGAATGGGAAGCTTTTGCCCGGGGAACCAAAGCTCTCATGGATGAGGTGGTG
AAAGCCACTTCTAGGGGCTGCATCACCATCATAGGTGGTGGAGACACTGCCACTTGCTGT
GCCAAATGGAACACGGAGGATAAAGTCAGCCATGTGAGCACTGGGGGTGGTGCCAGTTTG
GAGCTCCTGGAAGGTAAAGTCCTTCCTGGGGTGGATGCTCTCAGCAATATTTAG

1. Michelson AM, Markham AF, Orkin SH: Isolation and DNA sequence of a full-length cDNA clone for human X chromosome-encoded phosphoglycerate kinase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):472-6. [PubMed ]
2. Michelson AM, Blake CC, Evans ST, Orkin SH: Structure of the human phosphoglycerate kinase gene and the intron-mediated evolution and dispersal of the nucleotide-binding domain. Proc Natl Acad Sci U S A. 1985 Oct;82(20):6965-9. [PubMed ]
3. Singer-Sam J, Keith DH, Tani K, Simmer RL, Shively L, Lindsay S, Yoshida A, Riggs AD: Sequence of the promoter region of the gene for human X-linked 3-phosphoglycerate kinase] Gene. 1984 Dec;32(3):409-17. [PubMed ]
4. Pfeifer GP, Steigerwald SD, Mueller PR, Wold B, Riggs AD: Genomic sequencing and methylation analysis by ligation mediated PCR. Science. 1989 Nov 10;246(4931):810-3. [PubMed ]
5. Huang IY, Welch CD, Yoshida A: Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence. J Biol Chem. 1980 Jul 10;255(13):6412-20. [PubMed ]
6. Jindal HK, Vishwanatha JK: Functional identity of a primer recognition protein as phosphoglycerate kinase. J Biol Chem. 1990 Apr 25;265(12):6540-3. [PubMed ]
7. Yoshida A: Hematologically important mutations: molecular abnormalities of phosphoglycerate kinase. Blood Cells Mol Dis. 1996;22(3):265-7. [PubMed ]
8. Yoshida A, Twele TW, Dave V, Beutler E: Molecular abnormality of a phosphoglycerate kinase variant (PGK-Alabama). Blood Cells Mol Dis. 1995;21(3):179-81. [PubMed ]
9. Cohen-Solal M, Valentin C, Plassa F, Guillemin G, Danze F, Jaisson F, Rosa R: Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes: PGK Creteil and PGK Amiens. Blood. 1994 Aug 1;84(3):898-903. [PubMed ]
10. Ookawara T, Dave V, Willems P, Martin JJ, de Barsy T, Matthys E, Yoshida A: Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant. Arch Biochem Biophys. 1996 Mar 1;327(1):35-40. [PubMed ]
11. Valentin C, Birgens H, Craescu CT, Brodum-Nielsen K, Cohen-Solal M: A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish patient with isolated chronic hemolytic anemia: mechanism of mutation and structure-function relationships. Hum Mutat. 1998;12(4):280-7. [PubMed ]
12. Maeda M, Yoshida A: Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue) associated with hemolytic anemia: Leu----Pro substitution caused by T/A----C/G transition in exon 3. Blood. 1991 Mar 15;77(6):1348-52. [PubMed ]
13. Maeda M, Bawle EV, Kulkarni R, Beutler E, Yoshida A: Molecular abnormalities of a phosphoglycerate kinase variant generated by spontaneous mutation. Blood. 1992 May 15;79(10):2759-62. [PubMed ]
14. Fujii H, Krietsch WK, Yoshida A: A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK Munchen) associated with enzyme deficiency. J Biol Chem. 1980 Jul 10;255(13):6421-3. [PubMed ]
15. Huang IY, Fujii H, Yoshida A: Structure and function of normal and variant human phosphoglycerate kinase. Hemoglobin. 1980;4(5-6):601-9. [PubMed ]
16. Fujii H, Kanno H, Hirono A, Shiomura T, Miwa S: A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria. Blood. 1992 Mar 15;79(6):1582-5. [PubMed ]
17. Fujii H, Chen SH, Akatsuka J, Miwa S, Yoshida A: Use of cultured lymphoblastoid cells for the study of abnormal enzymes: molecular abnormality of a phosphoglycerate kinase variant associated with hemolytic anemia. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2587-90. [PubMed ]
18. Fujii H, Yoshida A: Molecular abnormality of phosphoglycerate kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5461-5. [PubMed ]