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2.
J Med Genet ; 36(7): 524-31, 1999 Jul.
Article in English | MEDLINE | ID: mdl-10424812

ABSTRACT

In this study, we have examined CDKN1C expression in BWS patients with allele imbalance (AI) affecting the 11p15 region. Two of two informative patients with AI, attributable to mosaic paternal isodisomy, exhibited reduced levels of CDKN1C expression in the liver and kidney, respectively, relative to expression levels in the equivalent tissues in normal controls. Although overall expression was reduced, some expression from the paternally derived CDKN1C allele was evident, consistent with incomplete paternal imprinting of the gene. One patient showed evidence of maternal allele silencing in addition to AI. These findings show for the first time that CDKN1C expression is reduced in BWS patients with AI and suggest that CDKN1C haploinsufficiency contributes to the BWS phenotype in patients with mosaic paternal isodisomies of chromosome 11.


Subject(s)
Alleles , Beckwith-Wiedemann Syndrome/genetics , Chromosomes, Human, Pair 11 , Gene Expression Regulation , Nuclear Proteins/genetics , Cyclin-Dependent Kinase Inhibitor p57 , DNA Mutational Analysis , Genomic Imprinting , Genotype , Humans , Mosaicism/genetics , Polymerase Chain Reaction
3.
Pathology ; 30(4): 381-5, 1998 Nov.
Article in English | MEDLINE | ID: mdl-9839313

ABSTRACT

Recently, a new recurrent translocation, t(12;21)(p13;q22), has been identified in B-cell lineage acute lymphoblastic leukemia (ALL). The translocation results in the fusion of two known genes, ETV6/TEL(12p13) and AML1(21q22), both of which have been shown to be involved in other hematological malignancies. The t(12;21) is virtually undetectable by routine cytogenetics, but the chimeric transcript ETV6-AML1 has been detected in childhood ALL by molecular techniques in up to 36% of cases, making it the most common genetic abnormality in these patients. It has been shown to be associated with a B-precursor phenotype and an excellent prognosis. We tested 66 diagnostic pediatric ALL samples by reverse transcription polymerase chain reaction (RT-PCR) and found evidence of the t(12;21) in 22 (33%). None of these had previously been identified as harboring the t(12;21), although six had karyotypic abnormalities involving either 12p13 or 21q22. ETV6-AML1 expression defined a subgroup of patients characterised by an age of between two and 12 years, B-lineage immunophenotype and non-hyperdiploid DNA content. Our data further support the importance of molecular diagnostic methods in the identification of clinically distinct subgroups of patients with ALL.


Subject(s)
Chromosomes, Human, Pair 12/genetics , Chromosomes, Human, Pair 21/genetics , DNA, Neoplasm/analysis , Precursor Cell Lymphoblastic Leukemia-Lymphoma/genetics , Translocation, Genetic/genetics , Child , Child, Preschool , DNA Primers/chemistry , Female , Gene Expression Regulation, Neoplastic , Humans , Male , Precursor Cell Lymphoblastic Leukemia-Lymphoma/drug therapy , Precursor Cell Lymphoblastic Leukemia-Lymphoma/pathology , Reverse Transcriptase Polymerase Chain Reaction , Treatment Outcome
4.
Oncogene ; 12(5): 1005-14, 1996 Mar 07.
Article in English | MEDLINE | ID: mdl-8649791

ABSTRACT

The response of the CML-BC cell line, K562, the myelomonocytic cell line MM6 and the promyelocytic leukaemia cell line HL-60, to a 15 mer WT1 antisense oligonucleotide, targeted to the translation initiation site of the WT1 mRNA was examined. K562 cells exposed to 0.4 microM antisense oligonucleotide showed markedly reduced proliferation which was associated with reduced cell viability. Sense, scrambled and mutant antisense oligonucleotides had no effect on the proliferation of K562 cells. MM6 cells exposed to 0.4 microM antisense oligonucleotide also showed significantly reduced cellular proliferation which was also accompanied by loss of cell viability. In the K562 and MM6 antisense cultures that exhibited reduced cell viability, both DNA fragmentation and morphological features consistent with apoptosis could be identified. In contrast the growth of HL-60 cells was unaffected by exposure to 0.4 microM antisense oligonucleotide. In each of the cell lines examined, WT1 antisense oligonucleotide abrogated WT1 protein expression, and analysis of WT1 coding sequence in these cells showed that no oncogenic point mutations in the gene were present. We propose therefore that in some myeloid leukaemia cell lines, the expression of a normal WT1 protein is necessary for cell proliferation and that it plays a role in maintaining the viability of some leukaemia cells.


Subject(s)
Apoptosis/genetics , Blast Crisis/pathology , DNA-Binding Proteins/metabolism , Genes, Wilms Tumor/physiology , Leukemia, Myelogenous, Chronic, BCR-ABL Positive/pathology , Oligonucleotides, Antisense/pharmacology , Transcription Factors/metabolism , Base Sequence , Blast Crisis/genetics , Cell Differentiation/drug effects , Cell Differentiation/genetics , Cell Division/drug effects , Cell Division/genetics , DNA, Neoplasm/analysis , DNA-Binding Proteins/genetics , Flow Cytometry , Genes, Wilms Tumor/genetics , HL-60 Cells/drug effects , HL-60 Cells/pathology , Humans , Leukemia, Myelogenous, Chronic, BCR-ABL Positive/genetics , Molecular Sequence Data , Oligonucleotides, Antisense/genetics , Polymerase Chain Reaction , RNA, Messenger/metabolism , Sequence Analysis, DNA , Transcription Factors/genetics , WT1 Proteins
5.
Eur J Cancer ; 31A(13-14): 2270-6, 1995 Dec.
Article in English | MEDLINE | ID: mdl-8652255

ABSTRACT

Using a reverse transcriptase polymerase chain reaction to examine alternate splicing at site I (exon 5) and site II (exon 9) in the Wilms' tumour suppressor gene, WT1, we found that in seven of the 10 Wilms' tumours examined, splicing at site I was disrupted. This is predicted to result in isoform imbalance in Wilms' tumours, with an increase in isoforms in which the 17 amino acids encoded by exon 5 are missing. These observations could not be explained by mutations or rearrangements in flanking introns. Disrupted alternate splicing of exon 5 may play a role in the aetiology of Wilms' tumour.


Subject(s)
Alternative Splicing , Exons/genetics , Genes, Wilms Tumor/genetics , Kidney Neoplasms/genetics , Wilms Tumor/genetics , Animals , Base Sequence , Exons/physiology , Humans , Kidney Neoplasms/metabolism , Mice , Molecular Sequence Data , RNA, Messenger/genetics , RNA, Neoplasm/genetics , Wilms Tumor/metabolism
6.
Hum Mutat ; 5(3): 221-7, 1995.
Article in English | MEDLINE | ID: mdl-7599632

ABSTRACT

We have examined a panel of 21 sporadic Wilms' tumours for rearrangements in the Wilms' tumour suppressor gene, WT1. In one tumour with specific allele loss in chromosome 11p13, a homozygous deletion in the 3' end of the gene, encompassing exon 10 and the 3' untranslated region, was identified. High levels of a truncated WT1 transcript, predicted to encode a polypeptide missing the fourth zinc finger were expressed in this tumour. All other samples showed normal patterns of digestion on Southern blots. This observation confirms previous findings that large deletions in the gene occur infrequently in sporadic Wilms' tumours and that the zinc-finger region of the encoded polypeptide is critical for correct functioning of the gene.


Subject(s)
DNA-Binding Proteins/genetics , Gene Expression Regulation, Neoplastic , Kidney Neoplasms/genetics , Sequence Deletion , Transcription Factors/genetics , Wilms Tumor/genetics , Base Sequence , Blotting, Northern , Blotting, Southern , Chromosomes, Human, Pair 11/genetics , DNA-Binding Proteins/biosynthesis , Female , Humans , Male , Molecular Sequence Data , Restriction Mapping , Transcription Factors/biosynthesis , WT1 Proteins , Zinc Fingers
7.
Hum Mol Genet ; 2(12): 2089-92, 1993 Dec.
Article in English | MEDLINE | ID: mdl-8111378

ABSTRACT

We have examined insulin-like growth factor 1 receptor (IGF1R) gene expression for evidence of imprinting in 15 informative patients with embryonal tumours. Biallelic expression was observed in all but one sample of normal juvenile kidney and liver, and in 9/10 associated Wilms' tumours, 3/3 hepatoblastomas and 2/2 adrenal tumours. A single patient with Beckwith-Wiedemann Syndrome (BWS) demonstrated monoallelic expression of the maternally derived IGF1R allele in normal kidney, associated Wilms' tumour and in peripheral blood lymphocytes. The observed biallelic expression of the IGF1R gene in all but one patient strongly suggests that the human gene is not normally imprinted.


Subject(s)
Adrenal Glands/metabolism , Alleles , Gene Expression , Kidney/metabolism , Liver/metabolism , Neoplasms/metabolism , Polymorphism, Genetic , Receptor, IGF Type 1/biosynthesis , Receptor, IGF Type 1/genetics , Adrenal Gland Neoplasms/genetics , Adrenal Gland Neoplasms/metabolism , Animals , Base Sequence , Beckwith-Wiedemann Syndrome/genetics , Beckwith-Wiedemann Syndrome/metabolism , Child , DNA Primers , Female , Genotype , Hepatoblastoma/genetics , Hepatoblastoma/metabolism , Humans , Kidney Neoplasms/genetics , Kidney Neoplasms/metabolism , Liver Neoplasms/genetics , Liver Neoplasms/metabolism , Male , Mice , Molecular Sequence Data , Neoplasms/genetics , Organ Specificity , Pedigree , Polymerase Chain Reaction , Reference Values , Repetitive Sequences, Nucleic Acid , Wilms Tumor/genetics , Wilms Tumor/metabolism
8.
Genes Chromosomes Cancer ; 8(2): 104-11, 1993 Oct.
Article in English | MEDLINE | ID: mdl-7504513

ABSTRACT

Tumor and constitutional chromosome arm 11p genotypes were compared in 6 hepatoblastoma (HB) patients and 2 adrenal adenoma (AA) patients, with one HB patient and both AA patients displaying clinical features associated with the Beckwith-Wiedemann syndrome (BWS). Using up to 14 chromosome 11 polymorphic markers, loss of constitutional heterozygosity (LOH) was demonstrated in both AA patients and in 4 of 6 HB patients. This identified three distinct and non-overlapping regions of 11p within which LOH occurred, which were defined as lying distal to the gamma-globin locus (11p15.5), proximal to the gamma-globin locus but distal to 11p13 (LOH being detected at 11p15.1), and restricted to the 11p13 region. Specific LOH within each 11p15 region was observed in HB, and this represents the first demonstration by a single study of LOH clearly affecting separate regions of chromosome band 11p15 in a particular tumor type. One AA showed LOH restricted to 11p13 loci, implicating the involvement of the WT1 gene. The second AA patient presented with genitourinary abnormalities and we therefore examined sequences coding for 3 zinc finger domains of WT1 in both AAs. No point mutations were identified in sequence from either patient. Nonetheless our results indicate that 3 separate 11p loci may be significant in the development of tumors which arise in association with BWS.


Subject(s)
Adenoma/genetics , Adrenal Gland Neoplasms/genetics , Chromosome Deletion , Chromosomes, Human, Pair 11 , Hepatoblastoma/genetics , Liver Neoplasms/genetics , Base Sequence , Beckwith-Wiedemann Syndrome/pathology , Blotting, Southern , Child, Preschool , DNA, Neoplasm/analysis , DNA, Neoplasm/isolation & purification , Female , Gene Rearrangement , Genes, Wilms Tumor/genetics , Genetic Markers , Humans , Infant , Infant, Newborn , Male , Middle Aged , Molecular Sequence Data , Polymerase Chain Reaction , Polymorphism, Restriction Fragment Length , Zinc Fingers/genetics
10.
Alcohol Clin Exp Res ; 16(5): 922-7, 1992 Oct.
Article in English | MEDLINE | ID: mdl-1443431

ABSTRACT

The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using kcat/Km values as an indication of substrate efficacy, medium-chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed 'high-Km' properties with respect to ethanol, and is expected to significantly contribute to 'first-pass' metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver 'low-Km' ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.


Subject(s)
Alcohol Dehydrogenase/isolation & purification , Ethanol/pharmacokinetics , Isoenzymes/isolation & purification , Stomach/enzymology , Alcohol Dehydrogenase/physiology , Animals , Electrophoresis, Polyacrylamide Gel , Isoelectric Focusing , Isoenzymes/physiology , Kinetics , Liver/enzymology , Papio
12.
Exp Eye Res ; 51(4): 419-26, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2209753

ABSTRACT

Bovine corneal aldehyde dehydrogenase was purified to homogeneity and characterized with aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit size of 65 kDa. Using kcat/Km values as an indication of substrate efficacy, aldehyde products of lipid peroxidation were recognized as the likely 'natural' substrates. Protein yields from enzyme purification, as well as electrophoretic analyses of crude and purified enzyme preparations, demonstrated that this enzyme is the major soluble protein in bovine cornea, and constitutes around 0.5% wet weight of tissue. A dual role in protecting the eye against UV-B light is proposed--oxidation of aldehydes generated by light induced lipid peroxidation, and the direct absorption of UV-B light by bovine corneal ALDH.


Subject(s)
Aldehyde Dehydrogenase/physiology , Cornea/enzymology , Ultraviolet Rays/adverse effects , Aldehyde Dehydrogenase/isolation & purification , Animals , Cattle , Cornea/radiation effects , Isoelectric Focusing , Kinetics , Solubility , Spectrophotometry, Ultraviolet
13.
Protein Expr Purif ; 1(1): 45-8, 1990 Sep.
Article in English | MEDLINE | ID: mdl-1983795

ABSTRACT

Dihydroorotate (DHO) synthetase is a trifunctional protein that catalyzes the first three reactions of de novo pyrimidine biosynthesis. A single-step procedure for purification of DHO synthetase from mutant hamster cells that overproduce this protein has been developed. The synthetase is adsorbed from a postmitochondrial supernatant to a column of Procion blue-Sepharose 4B and, after the column is washed, the synthetase is eluted as a single peak with 0.4 M KCl. Pooled fractions from the trailing side of this peak yield DHO synthetase with a specific activity for aspartate transcarbamylase of 14 mumol/min/mg protein, representing a purification factor of 8.5-fold and a recovery of 28% from the postmitochondrial supernatant. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the DHO synthetase was of high purity. A further 34% of the DHO synthetase from the leading side of the eluted peak contained a minor proportion of a proteolytic fragment. Similar results were obtained with an established four-step purification procedure.


Subject(s)
Aspartate Carbamoyltransferase/isolation & purification , Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/isolation & purification , Chromatography, Agarose/methods , Dihydroorotase/isolation & purification , Multienzyme Complexes/isolation & purification , Animals , Aspartate Carbamoyltransferase/chemistry , Aspartate Carbamoyltransferase/genetics , Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/chemistry , Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/genetics , Cell Line , Coloring Agents , Cricetinae , Dihydroorotase/chemistry , Dihydroorotase/genetics , Multienzyme Complexes/chemistry , Multienzyme Complexes/genetics , Mutation , Triazines
14.
Biochim Biophys Acta ; 995(2): 168-73, 1989 Apr 06.
Article in English | MEDLINE | ID: mdl-2930794

ABSTRACT

The major isozyme of aldehyde dehydrogenase in mouse stomach, AHD-4, has been purified to homogeneity and characterized with a range of aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit size of 65 kDa. Using V/Km values as an indication of substrate efficacy, aromatic aldehydes were the preferred substrates. The enzyme used either NAD+ or NADP+ as cofactor, but showed a preference for NAD+. AHD-4 showed 'high-Km' properties with respect to acetaldehyde, but differed from the 'high-Km' liver mitochondrial enzyme (AHD-1), in that it was not a semialdehyde dehydrogenase. The enzyme was significantly active towards the peroxidic aldehyde, 4-hydroxynonenal, and may play a role in vivo in the detoxification of aromatic aldehydes and the aldehyde products of lipid peroxidation.


Subject(s)
Aldehyde Dehydrogenase/isolation & purification , Isoenzymes/isolation & purification , Stomach/enzymology , Acetaldehyde/metabolism , Aldehyde Dehydrogenase/metabolism , Aldehydes/metabolism , Animals , Hydrogen-Ion Concentration , Isoelectric Point , Isoenzymes/metabolism , Kinetics , Liver/enzymology , Macromolecular Substances , Mice , Mice, Inbred C57BL , Mice, Inbred Strains , Molecular Weight , NAD/metabolism , NADP/metabolism , Substrate Specificity
15.
Biochemistry ; 28(2): 463-70, 1989 Jan 24.
Article in English | MEDLINE | ID: mdl-2565732

ABSTRACT

In mammals, dihydroorotase is part of a trifunctional protein, dihydroorotate synthetase, which catalyzes the first three reactions of de novo pyrimidine biosynthesis. Dihydroorotase catalyzes the formation of a peptide-like bond between the terminal ureido nitrogen and the beta-carboxyl group of N-carbamyl-L-aspartate to yield heterocyclic L-dihydroorotate. A variety of evidence suggests that dihydroorotase may have a catalytic mechanism similar to that of a zinc protease [Christopherson, R. I., & Jones, M. E. (1980) J. Biol. Chem. 255, 3358-3370]. Tight-binding inhibitors of the zinc proteases, carboxypeptidase A, thermolysin, and angiotensin-converting enzyme have been synthesized that combine structural features of the substrates with a thiol or carboxyl group in an appropriate position to coordinate a zinc atom bound at the catalytic site. We have synthesized (4R)-2-oxo-6-thioxohexahydropyrimidine-4-carboxylate (L-6-thiodihydroorotate) and have found that this analogue is a potent competitive inhibitor of dihydroorotase with a dissociation constant (Ki) in the presence of excess Zn2+ ion of 0.17 +/- 0.02 microM at pH 7.4. The potency of inhibition by L-6-thiodihydroorotate in the presence of divalent metal ions decreases in the order Zn2+ greater than Ca2+ greater than Co2+ greater than Mn2+ greater than Ni2+; L-6-thiodihydroorotate alone is less inhibitory and has a Ki of 0.85 +/- 0.14 microM. 6-Thioorotate has a Ki of 82 +/- 8 microM which decreases to 3.8 +/- 1.4 microM in the presence of Zn2+. Zn2+ alone is a moderate inhibitor of dihydroorotase and does not enhance the potency of other inhibitors.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Amidohydrolases/antagonists & inhibitors , Dicarboxylic Acids/chemical synthesis , Dihydroorotase/antagonists & inhibitors , Pyrimidines/chemical synthesis , Sulfhydryl Compounds/pharmacology , Animals , Binding, Competitive , Cations, Divalent , Cell Line , Cricetinae , Cysteine/analogs & derivatives , Cysteine/pharmacology , Dicarboxylic Acids/pharmacology , Dihydroorotase/isolation & purification , Indicators and Reagents , Kinetics , Magnetic Resonance Spectroscopy , Pyrimidines/pharmacology , Structure-Activity Relationship , Substrate Specificity
18.
Int J Biochem ; 18(1): 49-56, 1986.
Article in English | MEDLINE | ID: mdl-3943656

ABSTRACT

Liver cytosolic aldehyde dehydrogenases (AHD-2) have been isolated in a highly purified state from "alcohol-drinking" (C57BL/6J) and "alcohol-avoiding" (DBA/2J) strains of mice. The purified enzymes were resolved into three major and one minor form of activity by isoelectric focusing (IEF) techniques and showed similar zymogram patterns. The enzymes had identical subunit sizes on SDS-polyacrylamide gels: 53,000. Gel exclusion chromatography, using Ultrogel AcA34, indicated that the enzymes were dimers. The enzymes exhibited biphasic kinetic characteristics and were readily distinguished from each other. The purified forms of AHD-2 from C57BL/6J and DBA/2J mice exhibited two apparent Km values in each case: 10 microM/100 microM and 30 microM/330 microM respectively. AHD-2 exhibited a broad pH optimum in the range 7.0-9.0 and was very sensitive towards disulphuram inhibition, with 50% inhibition occurring at 0.17 microM. The kinetic results support proposals that AHD-2 may be the primary enzyme for oxidizing acetaldehyde during ethanol oxidation in vivo.


Subject(s)
Alcohol Drinking , Aldehyde Dehydrogenase/isolation & purification , Liver/enzymology , Aldehyde Dehydrogenase/analysis , Aldehyde Dehydrogenase/antagonists & inhibitors , Animals , Cytosol/enzymology , Disulfiram/pharmacology , Histocytochemistry , Hydrogen-Ion Concentration , Isoelectric Focusing , Kinetics , Mice , Mice, Inbred C57BL , Mice, Inbred DBA , Molecular Weight , Species Specificity
19.
Biochem J ; 228(3): 627-34, 1985 Jun 15.
Article in English | MEDLINE | ID: mdl-2992451

ABSTRACT

The three enzymes glucokinase (EC 2.7.1.2), fructokinase (EC 2.7.1.4) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) were isolated in high yield from extracts of Zymomonas mobilis. The principal steps in the isolation procedures involved the use of selected dye-ligand adsorbent columns, with affinity elution of two of the three enzymes. Glucokinase and fructokinase are dimeric proteins (2 X 33000 Da and 2 X 28000 Da respectively) and glucose-6-phosphate dehydrogenase is a tetramer (4 X 52000 Da). Some similarities in the structural and kinetic parameters of the two kinases were noted, but they have absolute specificity for their substrates. Fructokinase is strongly inhibited by glucose; otherwise non-substrate sugars had little effect on any of the three enzymes.


Subject(s)
Bacteria/enzymology , Fructokinases/metabolism , Glucokinase/metabolism , Glucosephosphate Dehydrogenase/metabolism , Phosphotransferases/metabolism , Adsorption , Carbohydrate Metabolism , Chromatography, Affinity , Electrophoresis, Polyacrylamide Gel , Fructokinases/isolation & purification , Glucokinase/isolation & purification , Glucosephosphate Dehydrogenase/isolation & purification , Kinetics , Macromolecular Substances , Substrate Specificity
20.
Int J Biochem ; 17(1): 51-60, 1985.
Article in English | MEDLINE | ID: mdl-3996732

ABSTRACT

Aldehyde dehydrogenase isozymes (AHD-1 and AHD-5) have been isolated in a highly purified state from extracts of mouse liver mitochondria. The enzymes have distinct subunit sizes, as determined by SDS/polyacrylamide gel electrophoresis: AHD-1, 63,000; AHD-5, 49,000. Gel exclusion chromatography, using sephadex G-200, indicated that both isozymes are dimers, although AHD-1 may also exist as a monomeric form as well. The enzymes exhibited widely divergent kinetic characteristics. The purified allelic forms of AHD-1, AHD-1A (C57BL/6J mice) and AHD-1B (CBA/H mice), exhibited high Km values with acetaldehyde as substrate, 1.4 mM and 0.78 mM respectively, whereas AHD-5 exhibited a low Km value with acetaldehyde of 0.2 microM. In addition, the isozymes exhibited distinct pH optima for catalysis (AHD-1, pH range 6.5-7.5; AHD-5, pH range 8.5-10.0), and were differentially sensitive towards disulphuram inhibition, with 50% inhibition occurring 13 and 0.1 microM for the AHD-1 and AHD-5 isozyme respectively. Based upon the kinetic characteristics, it is suggested that AHD-5 may be the primary enzyme for oxidizing mitochondrial acetaldehyde during ethanol oxidation in vivo.


Subject(s)
Aldehyde Dehydrogenase/isolation & purification , Mitochondria, Liver/enzymology , Aldehyde Dehydrogenase/antagonists & inhibitors , Aldehyde Dehydrogenase/metabolism , Animals , Disulfiram/pharmacology , Hydrogen-Ion Concentration , Isoelectric Point , Isoenzymes/antagonists & inhibitors , Isoenzymes/isolation & purification , Isoenzymes/metabolism , Kinetics , Mice , Molecular Weight
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