Inheritance of needle tissue isozymes in Douglas-fir

1984 ◽  
Vol 26 (4) ◽  
pp. 459-468 ◽  
Author(s):  
D. B. Neale ◽  
J. C. Weber ◽  
W. T. Adams
Keyword(s):  
Glutamate Dehydrogenase ◽  
Pseudotsuga Menziesii ◽  
Isocitrate Dehydrogenase ◽  
Seed Orchard ◽  
Douglas Fir ◽  
Glutamate Oxaloacetate Transaminase ◽  
Electrophoretic Variants ◽  
Phosphogluconate Dehydrogenase ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase

Methods for resolving electrophoretic variants from extracts of needle tissue of coastal Douglas-fir (Pseudotsuga menziesii var. menziesii (Mirb.) Franco) are described, and the inheritance of 12 of at least 15 loci that control allozymes from 11 enzyme systems are established. Evidence for the inheritance of allozyme variants was obtained in three ways: (i) comparison in seed orchard clones of allozyme genotypes determined from both megagametophyte and needle tissue; (ii) analysis of segregating full-sib progenies of seed orchard clones; and (iii) comparison of needle allozyme pattern phenotypes to previously reported embryo phenotypes. Ten of the 12 loci (coding phosphoglucomutase, PGM(1) and PGM(2); glycerate dehydrogenase, GLYDH; phosphoglucose isomerase, PG1(2); glutamate dehydrogenase, GDH; glucose-6-phosphate dehydrogenase, G-6PD; 6-phosphogluconate dehydrogenase, 6-PGD(1); isocitrate dehydrogenase, IDH; diaphorase, DIA(2); malate dehydrogenase, MDH(1)) produce clear bands in seed tissue; however, glutamate oxaloacetate transaminase GOT(3) (N) was not found in seeds and shikimic dehydrogenase (SDH) could only be clearly resolved in needles (N). Several enzymes active in seed tissue could not be detected in needle tissues.Key words: Douglas-fir, needle tissue isozymes, inheritance.

INHERITANCE OF ALLOZYME VARIANTS IN COASTAL DOUGLAS-FIR (PSEUDOTSUGA MENZIESII VAR. MENZIESII)

1982 ◽  
Vol 24 (3) ◽  
pp. 325-335 ◽  
Author(s):  
Y. A. El-Kassaby ◽  
F. C. Yeh ◽  
O. Sziklai
Keyword(s):  
Superoxide Dismutase ◽  
Acid Phosphatase ◽  
Pseudotsuga Menziesii ◽  
Malic Enzyme ◽  
Quaternary Structure ◽  
Allelic Variation ◽  
Enzyme System ◽  
Douglas Fir ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase

The inheritance of 27 loci from 18 enzyme systems was investigated using both megagametophyte and embryo tissues of open pollinated seed collected from a natural stand of coastal Douglas-fir [Pseudotsuga menziesii var. menziesii (Mirb.) Franco]. Four enzyme systems - glutamate dehydrogenase (GDH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), mannose-6-phosphate isomerase (MPI), and peptidase (PEP) - appeared to be monomorphic and the remaining 14 systems - acid phosphatase (APH), aconitase (ACO), aspartate aminotransferase (AAT), diaphorase (DIA), esterase (EST), glucose-6-phosphate dehydrogenase (G6P), hexoseaminidase (HA), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH), malic enzyme (ME), phosphoglucose isomerase (PGI), phosphoglucomutase (PGM), 6-phosphogluconic dehydrogenase (6-PGD), and superoxide dismutase (SOD)-showed polymorphism. Each enzyme system was discussed with respect to its multilocus organization, subunit (quaternary) structure, and allelic variation.

Constancy of enzyme electrofocusing patterns in a stand of the lichen Umbilicaria mammulata

1986 ◽  
Vol 64 (9) ◽  
pp. 1928-1934 ◽  
Author(s):  
C. Hageman ◽  
D. Fahselt
Keyword(s):  
Alkaline Phosphatase ◽  
Superoxide Dismutase ◽  
Glutamate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Mannitol Dehydrogenase ◽  
Specific Staining ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Sampling Times ◽  
Umbilicaria Mammulata

Thalli of the lichen Umbilicaria mammulata (Ach.) Tuck, were collected from one site, 24 at each of five different sampling times, over a period of 1 year. Protein extracts from each individual thallus were subjected to isoelectric focusing, followed by specific staining for eight enzyme systems (mannitol dehydrogenase, isocitrate dehydrogenase, 6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, superoxide dismutase, esterase, and alkaline phosphatase). A total of 55 bands were resolved, 25 of which were constant in all thalli through all sampling dates. Principal components analysis of the electromorph data showed the existence of groups corresponding to sets of thalli collected at the same times; esterase and alkaline phosphatase variation were primarily responsible for these groupings. Banding patterns of 6-phosphogluconate dehydrogenase and superoxide dismutase were constant regardless of date of collection. Most bands of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were consistent through all sampling times, but each system exhibited one band that differed in frequency from one collection date to another. Electromorphs of mannitol dehydrogenase and isocitrate dehydrogenase exhibited only minor variability. Dehydrogenase enzymes, since they tended to vary least from one sampling time to the next, can thus be used more readily for taxonomic purposes. If esterases and alkaline phosphatases are to be applied as taxonomic criteria, samples for comparison should be collected simultaneously.

scholarly journals Study of different isozymes in Pinus gerardiana Wall.

2019 ◽  
Vol 11 (1) ◽  
pp. 116-120
Author(s):  
Mamata Ranot ◽  
Rajesh Sharma
Keyword(s):  
Genetic Diversity ◽  
Glutamate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Shikimic Acid ◽  
Polymorphic Loci ◽  
Phosphogluconate Dehydrogenase ◽  
Acid Dehydrogenase ◽  
Enzyme Systems ◽  
Pinus Gerardiana

Pinus gerardiana (Chilgoza) is a small to medium sized evergreen tree yielding a highly valuable edible nut. The present investigations were undertaken to assess the different isozymes in Chilgoza pine. Seven isozymes viz., MDH (Malate dehydrogenase), GDH (Glutamate dehydrogenase), SKDH (Shikimic acid dehydrogenase), 6PGDH (6-Phosphogluconate dehydrogenase), MNR (Menadione reductase), IDH (Isocitrate dehydrogenase) and ADH (Alcohol dehdrogenase) were studied. A total of sixteen gene loci were recorded for seven enzyme systems out of which 6 loci namely MDH- A, 6PGDH- A, SKDH- A, IDH- B, MNR- B and ADH- A were polymorphic whereas the remaining ten gene loci i.e. MDH- B, MDH- C, MDH- D, GDH- A, 6PGDH- B, SKDH- B, IDH- A, MNR- A, MNR- B and ADH- B showed no variation. The percentage of polymorphic loci and average number of alleles per locus are one of the useful criterions for comparing species of populations for genetic diversity.

EINFLUSS VON CYCLUS UND EXOGENER HORMONZUFUHR AUF STOFFWECHSELVORGÄNGE DES RATTENUTERUS

1967 ◽  
Vol 56 (2) ◽  
pp. 231-243 ◽  
Author(s):  
H. Schmidt ◽  
I. Noack ◽  
H. Walther ◽  
K. D. Voigt
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Leucine Aminopeptidase ◽  
Intraperitoneal Administration ◽  
Exogenous Hormone ◽  
Rat Uterus ◽  
Normal Cycle ◽  
Phosphogluconate Dehydrogenase ◽  
Dna And Rna ◽  
Hormone Administration ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACT The first significant increase of weight, RNA and protein was observed in the uterus of spayed rats twelve hours after the intraperitoneal administration of a single dose of 1 μg oestradiol. There was no significant increase of DNA. At the same time the activities of glucose-6-phosphate dehydrogenase, fructose-1,6-diphosphate aldolase, isocitrate dehydrogenase and leucine aminopeptidase had increased significantly. Twentyfour hours after the injection the augmented values began to decline. Three injections of 1 μg oestradiol, given at 24 hour intervals obtained similar changes, the only difference being that these changes were more marked and that a DNA increase was also observed. The augmentation of protein, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and fructose-1,6-diphosphate aldolase content of cells induced by repeated oestradiol injections was inhibited partly by 1 mg progesterone when administered together with the last dose of oestradiol. During the normal oestrus cycle of the rat uterus an increase of uterine weight, DNA and RNA content and also of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and 1,6-diphosphate aldolase activities was observed, whereas isocitrate dehydrogenase, malate dehydrogenase and leucine aminopeptidase did not change significantly. It would appear that the changes after exogenous hormone administration reflect those of the normal cycle as regards both their extent and timing. The importance of these findings in connection with hormone-induced pathways of uterine metabolism is discussed.

scholarly journals The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria

1968 ◽  
Vol 107 (4) ◽  
pp. 455-465 ◽  
Author(s):  
C. Chapman ◽  
W Bartley
Keyword(s):  
Cytochrome C ◽  
Glutamate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Nadh Oxidase ◽  
Isocitrate Lyase ◽  
Lag Phase ◽  
Glutamate Oxaloacetate Transaminase ◽  
Oxoglutarate Dehydrogenase ◽  
Nadh Cytochrome ◽  
Glucose 6 Phosphate Dehydrogenase

1. Aerobically grown yeast having a high activity of glyoxylate-cycle, citric acid-cycle and electron-transport enzymes was transferred to a medium containing 10% glucose. After a lag phase of 30min. the yeast grew exponentially with a mean generation time of 94min. 2. The enzymes malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase and NADH–cytochrome c oxidoreductase lost 45%, 17%, 27% and 46% of their activity respectively during the lag phase. 3. When growth commenced pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, glutamate dehydrogenase (NADP+-linked) and NADPH–cytochrome c oxidoreductase increased in activity, whereas aconitase, isocitrate dehydrogenase (NAD+- and NADP+-linked), α-oxoglutarate dehydrogenase, fumarase, malate dehydrogenase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase, NADH oxidase, NADPH oxidase, cytochrome c oxidase, glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, isocitrate lyase and glucose 6-phosphate dehydrogenase decreased. 4. During the early stages of growth the loss of activity of aconitase, α-oxoglutarate dehydrogenase, fumarase and glucose 6-phosphate dehydrogenase could be accounted for by dilution by cell division. The lower rate of loss of activity of isocitrate dehydrogenase (NAD+- and NADP+-linked), glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, NADPH oxidase and cytochrome c oxidase implies their continued synthesis, whereas the higher rate of loss of activity of malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase and NADH oxidase means that these enzymes were actively removed. 5. The mechanisms of selective removal of enzyme activity and the control of the residual metabolic pathways are discussed.

scholarly journals Genetic diversity of seeds from four German Douglas fir (Pseudotsuga menziesii) seed orchards

2021 ◽  
Author(s):  
Birte Pakull ◽  
Pascal Eusemann ◽  
Janine Wojacki ◽  
Diana Ahnert ◽  
Heike Liesebach
Keyword(s):  
Genetic Diversity ◽  
Pseudotsuga Menziesii ◽  
Seed Orchard ◽  
Small Population ◽  
Douglas Fir ◽  
Next Generation ◽  
Seed Orchards ◽  
Population Sizes ◽  
Spatial Isolation ◽  
Offspring Generation

AbstractIn Germany, Douglas fir (Pseudotsuga menziesii Franco) is seen as a valuable species for future cultivation in times of climate change. Local seed production in seed stands and seed orchards may secure that local adaptation is transferred to the next generation, but small population sizes could lower genetic diversity and thus future adaptability. Here we analyse the transfer of genetic diversity from parent to offspring generation in four older German seed orchards. We detected low pollen contamination rates due to high levels of spatial isolation. Even with a relatively low number of 40 clones, seed orchard design with randomized and repeated planting of clones led to low selfing rates, and despite uneven parental contributions, the number of successful parents and the level of genetic intermixture were high enough to allow the transfer of an adequate part of the genetic diversity to the next generation. Larger numbers, however, might be needed to reliably conserve the entire genetic diversity over succeeding generations. Conclusions on the establishment of future seed orchards and regarding areas requiring further research are drawn at the end of the paper.

Morphological and biochemical characterization of the trypanosomatids Crithidia desouzai and Herpetomonas anglusteri

1991 ◽  
Vol 69 (3) ◽  
pp. 571-577 ◽  
Author(s):  
Maria Cristina M. Motta ◽  
Antonio M. Sole Cava ◽  
Paulo M. F. Silva ◽  
João E. Fiorini ◽  
Maurílio J. Soares ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Similarity Index ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Study ◽  
Monophyletic Cluster ◽  
Phosphogluconate Dehydrogenase ◽  
Unique Event ◽  
Enzyme Systems ◽  
Starch Gel ◽  
Glucose 6 Phosphate Dehydrogenase

Two species of trypanosomatids, Crithidia desouzai and Herpetomonas anglusteri, were recently isolated from Diptera in Minas Gerais, Brazil. The Crithidia species was found to harbor bacterium-like endosymbionts in the cytoplasm. To biochemically characterize these two species of trypanosomatids, and to try to verify the evolutionary meaning of the presence of endosymbionts, an electrophoretic study was undertaken whereby the two species were compared with eight other species in the same family. Horizontal 12.5% starch gel electrophoresis was used to resolve the isozymes of eight enzyme systems: acid phosphatase, glucose-6-phosphate dehydrogenase, hexokinase, malate dehydrogenase, malic enzyme, 6-phosphogluconate dehydrogenase, phosphoglucose isomerase, and phosphoglucomutase. Ten other enzyme systems were assayed without yielding any reproducible activity. The isozymes observed were conservatively interpreted as being due to the activity of 44 different alleles. All species studied differed in at least one enzyme system. The phenetic (Jaccard similarity index, UPGMA grouping) analysis produced a tree in which the species of Crithidia and Herpetomonas clustered separately, forming monophyletic groupings. All the endosymbiont-bearing species formed a monophyletic cluster, indicating that the presence of bacterium-like endosymbionts may be a synapomorphy of that group, and may represent, therefore, a unique event in the evolution of the genus.

TPNH GENERATION IN THE HUMAN OVARY

1965 ◽  
Vol 49 (1) ◽  
pp. 58-64 ◽  
Author(s):  
M. H. Nielson ◽  
J. C. Warren
Keyword(s):  
Life Cycle ◽  
Corpus Luteum ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Relative Activity ◽  
Human Ovary ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACT The endogenous activities of four major supernatant enzymes which produce TPNH (glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, malate dehydrogenase and isocitrate dehydrogenase) were quantitated in both normal and pathologic human ovarian tissues. The atrophic ovary demonstrated the lowest relative activity of the pentose shunt dehydrogenases, whereas luteinized tissues displayed the highest. During the course of its life cycle, the corpus luteum of the nonpregnant female displayed a progressive rise in isocitrate dehydrogenase and a concomitant fall in glucose-6-phosphate dehydrogenase activities. The corpus luteum of pregnancy, studied at term, demonstrated the highest levels of activity of all the four enzymes quantitated.

NADP-linked dehydrogenases in secreted milk

1985 ◽  
Vol 52 (4) ◽  
pp. 501-506 ◽  
Author(s):  
Murray R. Grigor ◽  
Peter E. Hartmann
Keyword(s):  
Mammary Gland ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Malic Enzyme ◽  
Prolonged Storage ◽  
Phosphogluconate Dehydrogenase ◽  
The Absolute ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Accurate Reflection

SUMMARYThe activities of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, isocitrate dehydrogenase, malic enzyme, lactate dehydrogenase and malate dehydrogenase have been determined in secreted milk from sows, rats and rabbits. Within each species, although there was considerable variation in the absolute activities of these enzymes, the relative activities were similar to those observed for, or previously published for mammary homogenates. The only exception was milk glucose 6-phosphate dehydrogenase which tended to lose activity upon prolonged storage in the mammary gland. These results suggest that the pattern of milk enzymes can be an accurate reflection of that occurring in the mammary gland.

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