Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0009443 (cold)
 92,137 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cattle brain cortex was homogenised in 0, 29 mol/1 sucrose and centrifuged at 101 000 X g. The supernatant contains the majority of 3 enzymes participating in protein turnover: cathepsin (EC 3.4.4.23), phosphoprotein phosphatase (EC 3.1.3.16) and acid phosphatase (EC 3.1.3.2). They were separated by chromatography on Sephadex G 200 in neutral buffer. The cathepsin was purified up to 380 fold by gel filtration on Sephadex and column electrophoresis. The pH optimum of cathepsin was 5.7. At 37 degrees C no decrease of activity was measurable during 30 min. The Km was found to be 2.75 mg/ml Casein Hammarsten. The molecular weight by gel filtration and exclusion-gel electrophoresis was about 45 000, corresponding to the cathepsin from human liver (Barrett, A.J. (1970) Biochem. J. 117, 601-607). The sedimentation constant 3.0 S20,W is comparable with the values of proteinase of different origin, and the composition is similar with respect to the high proportion of acidic amino acids. The phosphoprotein phosphatase can be further purified by chromatography on hydroxyapatite and by column electrophoresis. The pH optimum of phosphoprotein phosphatase was about pH 5.5. At 45 degrees C no decrease of activity was measurable during 20 min; the Km was 1.43 mg/ml casein isoelectric. The pH optimum of acid phosphatase was about 5.6. At 54 degrees C NO DECREASE OF ACTIVITY WAs measurable during 30 min; the Km was 2 mumol/1 for Sodium phenolphthalein diphosphate. All three enzymes slowly lost their activity during several weeks at - 4 degrees C, apparently by self digestion in the cold.
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PMID:[Cathepsin, phosphoprotein-phosphatase and acid phosphatase in the soluble fraction of the cattle brain cortex: purification and properties (author's transl)]. 0 48

A modified lysosomal fragility test is described which is suitable for use with cultured cells. The permeability (fragility) of the lysosomal membranes of the cells to the substrate beta-glycerophosphate is measured by assessing the degree of particulate lysosomal straining seen after exposing the cells to the Gomori acid phosphatase staining reaction under carefully controlled conditions. Monolayer cultures of endothelioid cells from the hearts of neonatal rats have been used in all experiments. The time-course of lysosomal straining for cells exposed to various treatments (normal saline, isotonic sucrose, 0.25 m sucrose, distilled water, acetate buffer pH 5.0, cold acetone, neutral formalin, acetic-ethanol, Triton X-100, hydrocortisone, choloroquine and vitamin A) was compared with that of control cells stained under identical conditions. Statistical differences in staining between the test and control cells were determined by the Wilcoxin Signed Rank Test and also by regression analysis following a transformation designed to allow for the saturation character of the reaction. The success of the modified technique depends upon meticulous methodology. It is capable of demonstrating both lysosomal membrane labilization and stabilation, second- and third-stage lysosomal activation, and apparent lysosomal enzyme loss or destruction in situ. The technique also allows the degree of reversible or first-stage lysosomal activation to be subdivided on an almost continous basis and is suitable for investigating the effects of drugs and other agents on the integrity of the lysosome in situ.
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PMID:The lysosomal permeability test modified for toxicity testing with cultured heart endothelioid cells. 4 54

Activities of acid phosphatase, beta-glucuronidase, N-acethyl-beta-D-glucosaminidase and acid beta-galactosidase were investigated histochemically in rabbit corneas. Frozen sections after block fixation in cold 4% formaldehyde with 1% CaCl2 followed by washing in cold physiological saline as well as cold microtome sections of corneas quenched in petroleter chilled with acetone-dry ice mixture, transferred to nonprecooled slides or semipermeable membranes were used. Standard aqueous media were employed in the case of free-floating frozen sections of fixed corneas as well as of cold mictrotome sections (postfixed in cold 4% formaldehyde). Agar media were used in connection with the technic of semipermeable membranes. Gomori method (in the case of acid phosphatase), simultaneous azocoupling methods (substrates derivated of naphthol-AS-BI with hexazonium-p-rosanilin) in the case of acid phosphatase, beta-glucuronidase and N-acetyl-beta-D-glucosaminidase and the indigogenic method in the case of acid beta-galactosidase were applied. Enzyme activities in sections of fixed corneas were minimal in comparison with those in cold microtome sections of unfixed material revealed particularly with the technic of semipermeable membranes which is to be preferred. This technic is recommended in studies concerned with lysosomal enzymes in the cornea, particularly in keratocytes. All enzymes investigated were present in corneal epithelium, keratocytes and endothelium. Acid phosphatase displayed the highest activity followed by beta-glucuronidase and acetyl-beta-D-glucosaminidase. The activity of beta-galactosidase was the lowest. For the demonstration of activities in keratocytes sections parallel to the surface are very suitable. In these sections enzyme activities were demonstrated in small granules (apparently lysosomes) present in the central part of their cytoplasm as well as in projections. Diffuse staining was also seen, being the highest in the case of acid phosphatase.
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PMID:Distribution of acid phosphatase, beta-glucuronidase, n-acetyl-beta-d-glucosaminidase and beta-galactosidase in cornea of albino rabbit. 5 44

The effects of fixation with various concentrations of glutaraldehyde or formaldehyde, acetone or ethanol, and freeze-drying on 5 phosphatases of Eimeria tenella and chick kidney cell cultures were demonstrated in situ. Gultaraldehyde inactivated the phosphatases more than did the formaldehyde, but the effect of the combination of the 2 (Karnovsky's fixative) was greater than that of either glutaraldehyde or formaldehyde alone. The higher the concentration of aldehyde and the longer the duration of exposure, the greater the inactivation. The order of sensitivity to aldehyde fixation of the enzymes tested was glucose-6-phosphatase greater than thiamine pyrophosphatase greater than 5'-nucleotidase greater than adenosine triphosphatase greater than acid phosphatase. Cytologic detail was preserved more efficiently with glutaraldehyde than with formaldehyde. Optimal preservation of enzyme activity for cytochemistry was with 2% glutaraldehyde for 30 min or 2% formaldehyde for 1 hr for G-6-Pase, TPPase, and 5'-nucleotidase, and with 2% glutaraldehyde or 2% formaldehyde for 2 hr with ATPase and AcPase. Quenching with subsequent fixation in cold acetone or ethanol resulted in complete inactivation of G-6-Pase, TPPase, and 5'-nucleotidase; although cells fixed in this manner yielded large amounts of reaction product for ATPase and AcPase, the distribution was diffuse, and some of it appeared to be artifactual. Quenching with subsequent freeze-drying was unsatisfactory because nearly all of the cell layers rolled off the cover glasses.
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PMID:Effect of fixation on demonstration of phosphatases of Eimeria tenella grown in chick kidney cell cultures. 6 Dec 71

Undecalcified bone and cartilage tissue blocks were fixed for 3 h in cold formol-calcium, rapidly dehydrated with a graded series of cold ethanol, and embedded in glycol methacrylate. 2 mum sections were produced with a Sorvall JB-4 microtome using glass knives. The quality of the sections were usually excellent except for hard bone from old subjects where the bone sometimes shattered while sectioning. This method is short, relatively uninvolved and eliminates en bloc decalcification. Moreover, the method is gentle enough to allow the histochemical demonstration of alkaline and acid phosphatase by the azo dye methods, and acid phosphatase, 5'-nucleotidase and ATPase by the lead precipitation methods.
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PMID:Enzyme histochemistry of undecalcified bone and cartilage embedded in glycol methacrylate. 17 7

A modification of Gomori's sulfide method for the determination of acid phosphatase activity is presented, which visualizes the walls of all capillaries in the myocardium, skeletal muscles, synovial membranes, and some other organs (liver, kidney). Blocks of investigated organs (edge lengths 2--3 mm) are cold-fixed in acetone for 2--3 days. Fixed frozen tissues are cut to sections 90--120 micrometer thick and incubated for 2--3 days in an incubation mixture (1% lead/II) acetate, 90 ml; acetate buffer solution pH 6.2, 10 ml; 2% sodium beta-glycerophosphate 1 ml. The sections are then processed with 0.5% sodium sulfide solution for 10--15 min and embedded into glycerine-gelatin gel. In preparations processed in this way, acid phosphatase is visualized on the walls of all capillaries and precapillaries, makig visible the capillary network. In addition to the capillaries, the transverse striation of myofibrils is visualized as well. The described method is useful for investigating not only the cytochemistry of the vascular wall, but also the blood supply to the myocardium, skeletal muscles, and other organs in both normal and pathological states.
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PMID:Investigations of capillary network in the myocardium, skeletal muscles, and other organs by modified Gomori's method for determination of acid phosphatase activity. 59 9

The relationship between the antifertility effect of alpha-chlorohydrin and changes in composition of luminal plasma from the cauda epididymidis of rats and rabbits has been investigated. At each dose regimen studied, the fertilizing capacity of rats treated with alpha-chlorohydrin was reduced to zero. The levels of sodium, potassium, glycerylphosphorylcholine (GPC), acid phosphatase and alkaline phosphatase in epididymal plasma were not markedly affected by drug treatment. The most noticeable change was a considerable increase in the concentration of lactic dehydrogenase (LDH) at all dose levels and of glutamic-oxaloacetic transaminase (GOT) after 7 days of treatment with 8 and 16 mg/kg. The effect of cold shock on the composition of epididymal plasma showed that LDH and GOT are, at least in part, derived from spermatozoa. In contrast, alpha-chlorohydrin did not have an antifertility action in the rabbit, and the only notable change in the compositon of epididymal plasma was an increase in the level of GPC. These results provide evidence that, in the rat, alpha-chlorohydrin or a metabolite primarily exerts its antifertility effect by a direct action on the spermatozoa, whilst in the rabbit a barrier may exist to the entrance of the drug into the lumen of the epididymal duct.
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PMID:The effects of alpha-chlorohydrin on the composition of rat and rabbit epididymal plasma: a possible explanation of species difference. 119 43

Enzyme cytochemistry was used to investigate possible lysosome involvement in capsaicin induced degranulation of the eosinophilic granule cell (EGC) of the rainbow trout intestine. Three adult rainbow trout (Oncorhynchus mykiss) were injected intraperitoneally with capsaicin in a saline vehicle (0.5 micrograms.g-1 body weight). Following a 2 hour period of incubation, the fish were killed, and a mid portion of the intestine was dissected and fixed in cold glutaraldehyde buffered with sodium cacodylate. Vibratome sections were incubated in either reaction medium containing beta-glycerophosphate and cerium chloride in acetate buffer or substrate (beta-glycerophosphate) deficient control medium. Sections were then refixed in osmium tetroxide and processed for electron microscopy. Acid phosphatase was found to be localised within lysosomes. The enzyme was not found in the large cytoplasmic granules under normal or capsaicin-stimulated conditions. EGCs which had migrated to the lamina propria in response to the capsaicin stimulation had a distinct multivesicular granule morphology. These multivesicular granules did not contain acid phosphatase suggesting that this form of EGC degranulation is not a lysosomally mediated event.
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PMID:Ultrastructural localisation of acid phosphatase in intestinal eosinophilic granule cells (EGC) of rainbow trout (Oncorhynchus mykiss) following degranulation with capsaicin. 151 13

The activities of aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), acid phosphatase (ACP), lactate dehydrogenase (LDH) and isocitric dehydrogenase (ICD) in the serum of 60 healthy dromedary camels of either sex and different ages (one to 25 years) were determined. The results were analysed with respect to time of year (December-January and May-June), sex and age groups (below four years; four to 10 years; and over 10 years). The overall mean activities of AST, ALT, ALP, ACP, LDH and ICD were 36.1 +/- 0.35, 4.65 +/- 0.35, 27.21 +/- 0.43, 7.18 +/- 0.21, 479.0 +/- 7.33 and 7.74 +/- 0.17 iu litre-1, respectively. Activities of AST, ALT, ALP and ACP were significantly higher during extremely hot conditions (May-June) than in extreme cold (December-January) while the activity of LDH was higher in extremely cold conditions. Analysis of data based on sex revealed that AST, ALT and ALP activities in the serum of male animals were significantly higher than in female animals. The activities of all the enzymes were highest in animals under four years and then gradually decreased with age being lowest in the animals over 10 years.
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PMID:Activity of some enzymes in the serum of dromedary camels. 166 69

The lysosomal proteolytic capacity of mouse brown adipose tissue (BAT) and its role during fasting were evaluated. The specific activities of acid phosphatase and cathepsins B, D, H, and L were measured in BAT of mice acclimated at 33, 21, and 4 degrees C and in BAT undergoing different rates of protein loss during a 24- to 48-h fast. The specific activities of lysosomal proteases in BAT did not vary with the acclimation status of the animals. Mice acclimated at 33 degrees C showed no significant atrophy of BAT after a fast. In mice kept at 21 degrees C, protein loss from BAT was observed after a fast without change in tissue DNA content. Protein loss from BAT was partially reduced by injection of the acidotropic agent chloroquine. Furthermore, tyrosine release from BAT during fasting was also reduced by injections of chloroquine or leupeptin, a thiol-protease inhibitor. Tyrosine release from BAT was maximum within 24 h and returned to prefast values by 36 h, suggesting rapid activation followed by inhibition of the tissue proteolytic activity. However, there was no change in acid protease specific activities, suggesting that these enzymes were not limiting for protein degradation. When cold-acclimated mice were fasted at 21 degrees C, BAT protein loss was markedly enhanced and increases in cathepsin D and L activities were observed, but there was no change in cathepsin B and H and acid phosphatase specific activities. These results indicate that BAT contains an important lysosomal proteolytic pathway that is involved in the rapid reduction of the tissue thermogenic capacity during a fast.
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PMID:Role of acid proteases in brown adipose tissue atrophy caused by fasting in mice. 218 82


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