المؤلفون: Yingying Shao, Hanlin Liu, Fangshun Li

المصدر: Biochemical genetics. 60(2)

مصطلحات موضوعية: Angiogenesis, Lactate dehydrogenase A, Biology, Biochemistry, Flow cytometry, Mice, Stomach Neoplasms, Genetics, medicine, Gene silencing, Animals, Humans, Radiosensitivity, Viability assay, education, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Cell Proliferation, Tube formation, Gene knockdown, education.field_of_study, medicine.diagnostic_test, L-Lactate Dehydrogenase, General Medicine, RNA, Circular, MicroRNAs, Cancer research, Lactate Dehydrogenase 5

الوصف: Earlier studies have shown that circular RNA (circRNA) expression is closely related to the malignant progression of cancer, but the role of circ-DONSON in gastric cancer (GC) has not been fully elucidated. The expression of circ-DONSON, miR-149-5p and lactate dehydrogenase A (LDHA) was measured via qRT-PCR. CCK8 assay was used to assess cell viability, and colony formation assay was performed to detect the number of colonies and the radiosensitivity of cells. Besides, flow cytometry, transwell assay and tube formation assay were employed to determine cell apoptosis, migration, invasion and angiogenesis. Western blot analysis was used to assess the protein expression. The interaction between miR-149-5p and circ-DONSON or LDHA was confirmed by dual-luciferase reporter assay. The influence of circ-DONSON on GC tumor growth in vivo was explored through constructing mice xenograft models. Our results suggested that circ-DONSON was highly expressed in GC tissues and cells. Loss-functional assay results confirmed that silenced circ-DONSON could inhibit the proliferation, metastasis and angiogenesis, while enhance the apoptosis and radiosensitivity of GC cells. In terms of mechanism, circ-DONSON could sponge miR-149-5p, which could target LDHA in GC. MiR-149-5p inhibitor or LDHA overexpression could reverse the suppression effect of circ-DONSON knockdown on GC progression. Additionally, our results also suggested that circ-DONSON silencing could restrain the tumor growth of GC in vivo. These results demonstrated that circ-DONSON could facilitate GC progression by increasing LDHA expression via sponging miR-149-5p, indicating that circ-DONSON might be a novel biomarker for GC treatment.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::413d6b6919aea0159759545bc02eac7cTest
https://pubmed.ncbi.nlm.nih.gov/34409524Test

المؤلفون: Walter Pretsch, Siegbert Merkle

المصدر: Biochemical genetics. 30(1-2)

مصطلحات موضوعية: Male, Erythrocytes, Lactate dehydrogenase A, Mutant, Biology, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, Mice, Lactate dehydrogenase, Genetics, medicine, Animals, education, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Crosses, Genetic, chemistry.chemical_classification, Mutation, education.field_of_study, Mice, Inbred C3H, L-Lactate Dehydrogenase, Isoelectric focusing, Point mutation, Muscles, General Medicine, Metabolism, Molecular biology, Enzyme, chemistry, Liver, Female, Spleen

الوصف: Two lactate dehydrogenase (LDH) mutations were recovered independently among offspring of ethylnitrosourea-treated male mice by screening for alterations of isoelectric focusing pattern in liver homogenates. Investigations of physicochemical and kinetic properties of the mutant enzymes indicated that the mutant traits resulted from point mutations at the Ldh-1 structural locus. Therefore, the new alleles were designated Ldh-1a-m5Neu and Ldh-1a-m6Neu, respectively. Both mutant alleles code for proteins which exhibit an altered stability to heat, in addition to changes in isoelectric focusing pattern and a reduction in anodal electrophoretic mobility. While LDH-Aa-m5Neu proteins are markedly less heat stable, LDH-Aa-m6Neu proteins are more heat stable than the wild-type enzyme. Furthermore, a small elevation of Km for pyruvate, a slightly reduced inhibition by high pyruvate concentrations, and a slight acidic shift of the pH activity profile distinguish LDH-Aa-m6Neu from both wild-type and LDH-Aa-m5Neu enzymes. Significant alterations of LDH activity were detected in some tissues from LDH-Aa-m5Neu individuals but not in those from LDH-Aa-m6Neu animals. Erythrocytes and blood of LDH-Aa-m5Neu mutants revealed activity levels which were reduced by approximately 6 and 13% compared with those of wild types in heterozygous and homozygous individuals, respectively. In addition, an elevation of approximately 6% in LDH activity was found in skeletal muscle in homozygous mutants. Consistent with the unaltered or only slightly altered LDH activity in tissues, the genetic as well as the physiological characterization yielded no easily detectable effects from either mutation on metabolism or fitness of the affected individuals.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57cec00badcbe613008d1f2bf61292f9Test
https://pubmed.ncbi.nlm.nih.gov/1520254Test

المؤلفون: Horst Spielmann, Joachim Klose

المصدر: Biochemical Genetics. 13:707-720

مصطلحات موضوعية: Male, C57BL/6, Macromolecular Substances, Polyacrylamide, Mice, Inbred Strains, Biology, Biochemistry, Isozyme, Mice, chemistry.chemical_compound, Lactate dehydrogenase, Testis, Genetics, Animals, Urea, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Mercaptoethanol, L-Lactate Dehydrogenase, Isoelectric focusing, Myocardium, General Medicine, biology.organism_classification, Molecular biology, Staining, Isoenzymes, Electrophoresis, Liver, chemistry, Organ Specificity, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing

الوصف: LDH of mouse organs (including testis) was investigated by isoelectric focusing in polyacrylamide gels. The number of LDH bands in this pattern considerably exceeds the five (six in testis) of the standard electrophoretic pattern. An attempt was made to identify these bands as tetrameric isoenzymes formed by random association of different subunits. This included isoelectric focusing of purified LDH A, B, and X, two-dimensional separation of LDH, urea treatment of LDH, staining with specific substrates, and comparison of different organs. Further experiments were performed to exclude artifacts possibly produced by the isoelectric focusing technique. Different strains of mice were also investigated. The results demonstrate that in addition to the common five LDH bands (A4−B4) one set of five bands is formed by LDH A (A 4 1 −A 4 2 ) and another one by LDH X (X 4 1 −X 4 2 ). Moreover, an unusual band was found which has a lower molecular weight and no affinity to the other isoenzymes. The data suggest that the heterogeneity of the LDH pattern revealed by isoelectric focusing arises from post-transcriptional events rather than from a number of additional genes.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bffba76d9a23228ea7c0c4046b6f2c1Test
https://doi.org/10.1007/bf00484928Test

المؤلفون: Leslie P. Kozak, Gordon K. McLean, Eva M. Eicher

المصدر: Biochemical Genetics. 11:41-47

مصطلحات موضوعية: Male, Genotype, Genetic Linkage, Electrophoresis, Starch Gel, Mice, Inbred Strains, Dehydrogenase, Glucosephosphate Dehydrogenase, Biology, Biochemistry, Chromosomes, Mice, chemistry.chemical_compound, Species Specificity, Pregnancy, Genetic linkage, Lactate dehydrogenase, Genetics, Animals, Molecular Biology, Gene, Crosses, Genetic, Ecology, Evolution, Behavior and Systematics, X chromosome, chemistry.chemical_classification, Phosphoglycerate kinase, Sex Chromosomes, L-Lactate Dehydrogenase, Genetic Variation, Embryo, General Medicine, Embryo, Mammalian, Molecular biology, Phosphoglycerate Kinase, Enzyme, chemistry, Female

الوصف: The levels of phosphoglycerate kinase (PGK), glucose 6-phosphate dehydrogenase (G6PD), and lactate dehydrogenase (LDH) were measured in one-cell embryos from X/0 and X/X females. Since the level of both PGK and G6PD was dependent on the number of X chromosomes present in the mother, these two enzymes are most likely coded for by X-linked genes. The level of LDH was the same in both types of embryos, indicating autosomal linkage. A search for an electrophoretic variant of PGK was not successful.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fe6b151690ae730004f22da0358bba7Test
https://doi.org/10.1007/bf00486618Test

المؤلفون: Shou-Mei T. Chang, Steven S.-L. Li, Chi-Yu Lee

المصدر: Biochemical Genetics. 17:715-729

مصطلحات موضوعية: Male, Protein Conformation, Protein subunit, Biochemistry, Isozyme, Mice, chemistry.chemical_compound, Affinity chromatography, Lactate dehydrogenase, Testis, Genetics, Animals, Amino Acids, Molecular Biology, Ecology, Evolution, Behavior and Systematics, chemistry.chemical_classification, L-Lactate Dehydrogenase, biology, Muscles, Myocardium, Tryptic peptide, Active site, General Medicine, Metabolism, Molecular biology, Amino acid, Isoenzymes, Molecular Weight, chemistry, Mice, Inbred DBA, biology.protein, Electrophoresis, Polyacrylamide Gel

الوصف: Three homotetrameric lactate dehydrogenase isozymes, LDH-M(A4), LDH-H(B4), and LDH-X(C4), from DBA/2J mice have been purified by affinity chromatography. The amino acid compositions of the subunits A,B, and C, based on a molecular weight of 36,000, have been determined. The compositional relatedness of these isozymes indicates that subunits A (muscle) and B (heart) are more closely related to each other than to subunit C (testis). Tryptic peptide maps and amino acid compositions of some active site peptides apear to confirm the compositional relatedness among these isozymes. The sequence of the loop region of mouse C subunit seems to be markedly different from all known A and B sequences, and the structural and functional implications are discussed.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6445f213cdf72658cc2eb25e56fc7258Test
https://doi.org/10.1007/bf00502130Test

المؤلفون: Daniel J. Charles, Walter Pretsch

المصدر: Biochemical Genetics. 19:301-309

مصطلحات موضوعية: Male, Heterozygote, Mutant, Mice, Inbred Strains, Biology, Biochemistry, Isozyme, Mice, chemistry.chemical_compound, Lactate dehydrogenase, Genetics, Animals, Allele, Molecular Biology, Polyacrylamide gel electrophoresis, Ecology, Evolution, Behavior and Systematics, L-Lactate Dehydrogenase, Isoelectric focusing, Homozygote, Wild type, General Medicine, Penetrance, Molecular biology, Pedigree, Isoenzymes, chemistry, Procarbazine, Mutation, Hybridization, Genetic, Female

الوصف: (101/El x C3H/el)F1 male mice were infected intraperitoneally with the mutagen procarbazine hydrochloride and immediately caged with untreated test-stock females. Crude liver extracts from the offspring were subjected to polyacrylamide gel isoelectric focusing, and the gels were stained for six enzymes. In the experimental group (mutagen treated spermatogonial germ-cell stage), a dominant inherited banding alteration of the lactate dehydrogenase (LDH) pattern was detected. By crossing the heterozygous mutants, homozygotes were obtained that showed much less gel staining intensity. The mutation is codominantly expressed with 100% penetrance. The banding alteration was also observed in muscle, kidney, heart, blood, brain, testis, spleen, and lung. Polyacrylamide gel electrophoresis was performed with all the tissues examined. The mutation causes the intensity of the band corresponding to LDH-A (primary molecular form in muscle) to decrease from that of the wild type, while the intensity of the bands corresponding to LDH-B (primary molecular form in heart) remains constant. It is concluded that the mutation affects the locus coding for LDH of the muscle type. Ldh-1c is proposed as the allele symbol.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c42e7d81798b11f878baa4a943715aeTest
https://doi.org/10.1007/bf00504275Test

المؤلفون: Charlotte M. Boone, Frank H. Ruddle

المصدر: Biochemical Genetics. 3:119-136

مصطلحات موضوعية: Electrophoresis, Pyruvate dehydrogenase kinase, Dehydrogenase, Glucosephosphate Dehydrogenase, In Vitro Techniques, Pyruvate dehydrogenase phosphatase, Biology, Biochemistry, Malate dehydrogenase, Mice, chemistry.chemical_compound, Malate Dehydrogenase, Lactate dehydrogenase, Genetics, Animals, Humans, Molecular Biology, Ecology, Evolution, Behavior and Systematics, L-Lactate Dehydrogenase, Esterases, Chromosome Mapping, General Medicine, Molecular biology, Isocitrate Dehydrogenase, Isoenzymes, Isocitrate dehydrogenase, chemistry, Karyotyping, Hybridization, Genetic, Phosphoglucomutase, Branched-chain alpha-keto acid dehydrogenase complex

الوصف: Human-mouse somatic cell hybrids have been isolated and examined for enzyme and chromosome constitution. The enzymes assayed were lactate dehydrogenase (LDH), isocitrate dehydrogenase (IDH), NADP-dependent malate dehydrogenase (MDH), glucose 6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD), phosphoglucomutase (PGM), and several esterases. Coexpression of mouse and human genomes and formation of heteropolymeric enzymes were observed in seven different hybrid populations for the enzymes LDH, IDH, MDH, and G6PD. Evidence predicated on the absence of chromosomal rearrangements is provided for the lack of genetic linkage in the human genome for these four enzymes, as well as for thymidine kinase.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52884bb7421036400f2470cb2b1fb012Test
https://doi.org/10.1007/bf00520348Test

المؤلفون: E.M. Tucker, A.R. Dain, R. A. Donker, S.W. Clarke

المصدر: Biochemical Genetics. 22:429-439

مصطلحات موضوعية: Locus (genetics), Hybrid Cells, Biochemistry, Isozyme, Superoxide dismutase, Mice, Gene mapping, Chromosome 19, Endopeptidases, Genetics, Animals, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Synteny, Chromosome 13, Hybridomas, L-Lactate Dehydrogenase, biology, Superoxide Dismutase, Chromosome Mapping, Chromosome, General Medicine, Molecular biology, Isoenzymes, biology.protein, Cattle

الوصف: A study correlating the presence of bovine isozymes in mouse myeloma/calf hybridomas with specific banded chromosomes of their bovine complement has enabled tentative assignments to be made of the bovine isozyme locus for peptidase C (PEP C) to chromosome 5 and the syntenic group lactate dehydrogenase B/peptidase B (LDH B/PEP B) to chromosome 19. There was some evidence for the association of LDH A with one of the last seven small pairs (23-29) of the complement and of superoxide dismutase 1 (SOD 1) with chromosome 13.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41833793a86cc45faa2ceb878097a7e8Test
https://doi.org/10.1007/bf00484514Test

المؤلفون: Robert J. Klebe

المصدر: Biochemical Genetics. 13:805-812

مصطلحات موضوعية: Erythrocytes, Serial dilution, Electrophoresis, Starch Gel, Analytical chemistry, Mice, Inbred Strains, Dehydrogenase, Biology, Biochemistry, Isozyme, Mice, Species Specificity, Genetics, Animals, Densitometer, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Mice, Inbred BALB C, Mice, Inbred C3H, End point, L-Lactate Dehydrogenase, Glucose-6-Phosphate Isomerase, Genetic Variation, Blood Proteins, General Medicine, Isoenzymes, Titer, Organ Specificity, Visible band, Densitometry

الوصف: Isozyme patterns may be analyzed quantitatively, without the use of a densitometer, by performing serial twofold dilutions of a sample to a visual end point. The specific activity (S) of a given dehydrogenase isozyme can be assessed in the presence of other isozymes catalyzing the same reaction, by (1) determining the isozyme titer (T) (defined as mg protein/ml in the last visible band) and (2) applying the formula S = K/T, where K is 1.6 X 10(-3) units/ml in the last visible band. The units/ml (U) in the starting material can be calculated from the equation U = K (2)n-1, where n is the number of the slot producing the last visible band.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc15f892ea0961918881aa4574b80c29Test
https://doi.org/10.1007/bf00484412Test

المؤلفون: Janice Britton, Louis Thaler

المصدر: Biochemical Genetics. 16:213-225

مصطلحات موضوعية: Mus spretus, Population, Zoology, Locus (genetics), Subspecies, Biochemistry, House mouse, Mice, Gene Frequency, Species Specificity, Genetics, Animals, education, Molecular Biology, Transaminases, Ecology, Evolution, Behavior and Systematics, education.field_of_study, L-Lactate Dehydrogenase, biology, Esterases, food and beverages, Blood Proteins, General Medicine, Reproductive isolation, biology.organism_classification, Isoenzymes, Genetics, Population, Genetic distance, Sympatric speciation, France, Oxidoreductases

الوصف: Populations of mice established outdoors as well as indoors have been investigated at 24 loci using starch gel electrophoresis. Two reproductively isolated groups are recognized, one of which is referable to a house mouse subspecies, Mus musculus brevirostris, and the other to a different species. Mus spretus, contrary to the view of Schwarz and Schwarz that only one species of Mus is present in the Mediterranean Basin. The genetic distance between these two groups is larger than between any pair of investigated subspecies of M. musculus. M. m. brevirostris is biochemically almost indistinguishable from M. m. domesticus. On the other hand, M. spretus exhibits several allelic variants unknown or at most very infrequent in M. musculus, as for instance at the lactate dehydrogenase B-chain locus.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40cfdb57724546b62ee73c4a8ecc02a3Test
https://doi.org/10.1007/bf00484079Test