Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The relationship between plasma protein bound iodine (PBI) level and creatine kinase (CK) activity was investigated in 143 males and 528 females suspected of various thyroid disorders; there was significant negative correlation between low PBI level and raised CK activity. CK, aldolase, lactate dehydrogenase (LD), aspartate transaminase (AST), and alanine transaminase (ALT) activities were determined in plasma from patients with reduced PBI levels; apart from CK, LD was the only enzyme increased in an appreciable number of cases. A further series of specimens was collected from 66 patients with low PBI levels and the CK isoenzymes investigated. In all of these MM was the main form present; a trace of MB was found in 6. These findings do not explain the elevation of CK in hypothyroidism which may be a non-specific effect.
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PMID:An investigation into creatine kinase and other plasma enzymes in thyroid disorders. 7 98

Specific antisera against glycogen phosphorylase, phosphofructokinase, aldolase, glyceraldehyde-phosphate dehydrogenase, enolase, lactate dehydrogenase, cytosolic and mitochondrial malate dehydrogenase from rabbit muscle were obtained from sheep. The gamma-globulins were used for indirect immunofluorescent localization of the respective enzymes in rabbit skeletal muscle and heart. In stretched skeletal muscle a cross-striation like distribution was observed for all enzymes studied. In the case of mitochondrial malate dehydrogenase this pattern is due to the staining of I-band mitochondria. In cross-sections, an intense staining of the sarcolemma and of subsarcolemmal mitochondria was observed. Comparative analyses with polarized light revealed that the cytosolic enzymes under study are distributed in the relaxed muscle fibre predominantly within the isotropic zones. The same distribution holds also for heart. In contracting muscle a decrease in cross-striated fluorescence and a faint staining of the interfibrillar spaces suggests a location also within the interfibrillar space.
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PMID:Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit. 12 16

The activity of the enzymes of glycolysis (phosphofructokinase, aldolase, pyruvate kinase, lactate dehydrogenase) and hexose monophosphate shunt (glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase) was determined in the eye tissues of the rabbit at different stages of ontogenesis. The activity of these enzymes in the retina was shown to be higher than in other eye tissues. In the uveal tract (iris, ciliary bodies, uvea) the activity of glycolytic enzymes changes with the age. The greatest changes in the activity of enzymes were found during the period of the opening of eyelids. The activity of the enzymes of hexose monophosphate shunt in the eye tissues increases with the age. The relative activity of dehydrogenases of the hexose monophosphate shunt after the establishment of visual function is, however, not high and does not exceed that of phosphofructokinase and pyruvate kinase in the eye tissues of the rabbit.
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PMID:[Glycolysis in the eye tissues of the rabbit in ontogeny. I. The enzymes of glycolysis and hexosemonophosphate shunt]. 14 40

ATPase activity of actomyosin and activity of glycogenolytic enzymes were distinctly increased during postnatal period of development. Direct correlation was observed between the actomyosin ATPase and phosphofructokinase, phosphohexoisomerase, enolase, pyruvate kinase, lactate dehydrogenase and "bound" fraction of aldolase. Kinetic patterns of phosphofructokinase (Km and Hill's coefficient) were not altered at the postnatal period. Formation of complexes between the contractile proteins and glycolytic enzymes appears to be important in development of contractile function.
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PMID:[Comparative study of the changes in the ATPase activity of actomyosin and in the activity of skeletal muscle glycolytic enzymes in the early postnatal period of development]. 14 21

The authors studied the histochemical and ultrastructural alterations of human muscles after spontaneous rupture of the tendon. Both succinate dehydrogenase (in type 1 fibres), and ATPase (in type 2 fibres) activity decreased in all injured muscles. In the intact antagonists and in contralateral muscles alterations were not found. The creatine phosphokinase and aldolase activity were decreased also in the injured muscles. The lactate dehydrogenase activity was various both in affected and in unaffected antagonists muscles. 2 weeks or more after the rupture of the tendon, in the injured muscles the number of type 1 fibres were decreased and therefore a statistically significant type 2 fibre predominance occurred. Ultrastructurally the disruption and disorientation of the myofibrils, streaming and disorganisation of Z line were found. The sarcolemma was arranged, the sarcoplasmic reticulum was dilated; both normal, pycnotic and enlarged mitochondria were observed. The motor end-plates were not discernible.
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PMID:Histochemical and ultrastructural study of human muscles after spontaneous rupture of the tendon. 15 81

The authors studied the histochemical alterations of human skeletal muscles after tenotomy and after spontaneous rupture of the tendon. Both succinate dehydrogenase (in type I fibers), and myofibrillar ATP-ase (in type 2 fibers) activity was decreased in all injured muscles. In the intact antagonists and contralateral muscles alterations were not found. The creatine phosphokinase and aldolase activity were decreased also in injured muscles. The lactate dehydrogenase activity was various both in affected and in unaffected muscles. Two weeks or more after the injury of the tendon in injured muscles the number of type 1 fibers were decreased and therefore a mathematically significant type 2 fibre predominance occurred. Atrophy involve both type 1 and type 2 fibers, but type 1 fibre atrophy was more pronunced as type 2 fibre atrophy.
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PMID:Enzyme histochemical alterations in human skeletal muscles after tenotomy and after spontaneous rupture of the tendon. 15 62

1. Procedures were developed for the extraction and assay of glycolytic enzymes from the epididymis and epididymal spermatozoa of the rat. 2. The epididymis was separated into four segments for analysis. When rendered free of spermatozoa by efferent duct ligation, regional differences in enzyme activity were apparent. Phosphofructokinase, glycerol phosphate dehydrogenase and glucose 6-phosphate dehydrogenase were more active in the proximal regions of the epididymis, whereas hexokinase, lactate dehydrogenase and phosphorylase were more active in the distal segment. These enzymes were less active in the epididymis of castrated animals and less difference was apparent between the proximal and distal segments. However, the corpus epididymidis from castrated rats had lower activities of almost all enzymes compared with other epididymal segments. 3. Spermatozoa required sonication to obtain satisfactory enzyme release. Glycolytic enzymes were more active in spermatozoa than in epididymal tissue, being more than 10 times as active in the case of hexokinase, phosphoglycerate kinase and phosphoglycerate mutase. 4. The specific activities of a number of enzymes in the epididymis were dependent on the androgen status of the animal. These included hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase, glycerol phosphate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and phosphorylase. 5. The caput and cauda epididymidis differed in the extent to which enzyme activities changed in response to an altered androgen status. The most notable examples were hexokinase, phosphofructokinase, aldolase, phosphoglycerate kinase, 6-phosphogluconate dehydrogenase and phosphorylase.
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PMID:Activity and androgenic control of glycolytic enzymes in the epididymis and epididymal spermatozoa of the rat. 18 56

In 28 dogs the distal articular cartilage of the femur was removed and the regenerating articular surface on the 70th postoperative day was studied histochemically for hexokinase, glucose-6-phosphatase, phosphohexose-isomerase, fructose-1, 6-diphosphatase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, lactate dehydrogenase isoenzymes, phosphoglucomutase, phosphorylase, glycogen synthetase, UDP--glucose dehydrogenase, and UDP-glucuronic acid-4-epimerase. The articular surface consisted of fibrous tissue and of cartilage islets. The latter contained cells differentiating into cartilage and young chondrocytes. The glycolytic enzymes reacted positively in the regenerative articular surface. Enzyme activities were higher in the cells (particularly the chondroblasts and young chondrocytes) of the cartilage islets than in the connective tissue. In the cells differentiations into cartilage, beside the LDH isoenzymes characteristic of glycolysis, a significant LDH1 and LDH2 activity was observed. At the same site the presence of fructose-1, 6-diphosphatase-activity could be assumed, but there was no glucose-6-phosphatase activity. Glycogen synthesis proceeded in the cells of the cartilage islets and UDP-glucuronic acid-4-epimerase activity was observed in the differentiated cells. UDP-glucose dehydrogenase activity was positive in every section of the articular surface.
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PMID:Studies on cartilage formation. XX. Histochemical investigation of some enzymes of glycogen metabolsim in regenerative articular surfaces. 18 10

Enzyme activity of lactate dehydrogenase, glutamate-oxalacetate and glutamate-pyruvate transaminase, creatine phosphokinase, cholinesterase, alkaline, acid and prostatic phosphatase and aldolase has been studied in a total of 213 subjects, of whom 97 were of good health, 63 had bone tumors and 53 suffered from osteomyelitis. The activities of the majority of the enzymes were found to become significantly changed in comparison with the norm. In both patient groups, the more striking differences being noted in that of osteomyelitis. However, enzymatic activity alone does not allow to differentiate the group of bone tumors from that of osteomyelitis, the differences between these two groups not being of significance in any one of the enzymes followed.
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PMID:Serum enzyme activity in bone tumors and osteomyelitis (LDH, GOT, GPT, CPK, CHE, ALP, AP, PP, ALD). 19 May 48

Interaction of several enzymes (pyruvate kinase, myokinase, creatine kinase, aldolase, malate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase and glucose-6-phosphate dehydrogenase) and other proteins (bovine serum albumin and ovalbumin) with Blue Dextran was studied by means of affinity electrophoresis in polyacrylamide gels. A decrease of electrophoretic mobility of enzymes in affinity gels was dependent on Blue Dextran concentration and in some cases, dissociation constants of the protein-immobilized dye complexes could be calculated. Affinity electrophoresis in the presence of Blue Dextran reveals in some cases additional bands of isoenzymes, as compared with the control gels (without Blue Dextran).
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PMID:Affinity electrophoresis of proteins interacting with Blue dextran. 20 48


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