scholarly journals Total Enzyme Syntheses of Napyradiomycins A1 and B1

2018 ◽  
Vol 140 (51) ◽  
pp. 17840-17845 ◽  
Author(s):  
Shaun M. K. McKinnie ◽  
Zachary D. Miles ◽  
Peter A. Jordan ◽  
Takayoshi Awakawa ◽  
Henry P. Pepper ◽  
...  
Keyword(s):  
Total Enzyme

METHODS OF PROTEIN EXTRACTION FROM NEUROSPORA CRASSA

1964 ◽  
Vol 10 (1) ◽  
pp. 29-35 ◽  
Author(s):  
G. J. Stine ◽  
W. N. Strickland ◽  
R. W. Barratt
Keyword(s):  
Glutamic Acid ◽  
Neurospora Crassa ◽  
Total Protein ◽  
Extraction Method ◽  
Protein Extraction ◽  
Specific Activity ◽  
Dry Weight ◽  
Acid Dehydrogenase ◽  
Total Enzyme

Nine methods for disrupting the mycelium of Neurospora crassa have been compared. Protein percentages are calculated per gram dry weight of mycelium. A TPN-specific glutamic acid dehydrogenase was extracted and the efficiency of each extraction method is given as total enzyme extracted and specific activity. In terms of total protein, total enzyme, and practicality of the method, the Hughes Press, the French Press and the Raper–Hyatt Press were found to be the most efficient. The advantages and limitations of each method are considered.

scholarly journals Growth-hormone-prolactin interactions in the regulation of mammary and adipose-tissue acetyl-CoA carboxylase activity and gene expression in lactating rats

1992 ◽  
Vol 285 (2) ◽  
pp. 469-475 ◽  
Author(s):  
M C Barber ◽  
M T Travers ◽  
E Finley ◽  
D J Flint ◽  
R G Vernon
Keyword(s):  
Adipose Tissue ◽  
Mammary Gland ◽  
Serum Prolactin ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Carboxylase Activity ◽  
Total Enzyme Activity ◽  
Mrna Concentration ◽  
Total Enzyme ◽  
Activation Status

The factors and mechanisms responsible for the reciprocal changes in lipogenesis in rat mammary gland and adipose tissue during the lactation cycle have been investigated. Lactation decreased the activation status and mRNA concentration of acetyl-CoA carboxylase in adipose tissue. Litter removal decreased the mRNA concentration of acetyl-CoA carboxylase in the mammary gland and increased the enzyme's mRNA concentration and activation status in adipose tissue. Lowering serum prolactin concentration in lactating rats decreased the amount of mammary acetyl-CoA carboxylase mRNA and increased that of adipose tissue, and increased the activation status of the enzyme in adipose tissue. Decreasing serum growth hormone (GH) alone had little effect on acetyl-CoA carboxylase in lactating rats, although it did lower pup growth rate and serum concentration of insulin-like growth factor-I. Lowering serum GH concentration exacerbated the effects of decreasing serum prolactin on mammary-gland (but not adipose-tissue) acetyl-CoA carboxylase mRNA and further increased the rise in activation status of the adipose-tissue enzyme induced by decreasing serum prolactin. Changes in acetyl-CoA carboxylase mRNA in both mammary and adipose tissue were paralleled by changes in total enzyme activity except after litter removal, when there was a disproportionately large decrease in total enzyme activity of the mammary gland. Thus prolactin has a major and GH a minor role in the regulation of acetyl-CoA carboxylase activity during lactation. Changes in mammary activity in response to prolactin and GH are primarily due to alterations in gene transcription, whereas adaptation in adipose tissue involves both changes in gene transcription and activation status.

Na-K-ATPase activity along the rabbit, rat, and mouse nephron

1979 ◽  
Vol 237 (2) ◽  
pp. F114-F120 ◽  
Author(s):  
A. I. Katz ◽  
A. Doucet ◽  
F. Morel
Keyword(s):  
Atpase Activity ◽  
Thick Ascending Limb ◽  
Sensitivity Limit ◽  
Henle's Loop ◽  
Collecting Tubule ◽  
Pars Recta ◽  
Hydrolysis Of ◽  
Total Enzyme

Na-K-ATPase activity along the rabbit, rat, and mouse nephron was determined with a micromethod that measures directly labeled phosphate released by the hydrolysis of [gamma-32P]ATP. Na-K-ATPase activity was highest in the rat, intermediate in the mouse, and lowest in the rabbit nephron. With the exception of rabbit cortical thick ascending limb, the enzyme profile was similar in the three species: Na-K-ATPase activity per millimeter tubule length was highest in the distal convoluted tubule and thick ascending limb of Henle's loop, intermediate in the proximal convoluted tubule, and lowest in the pars recta and collecting tubule. The enzyme was present in the thin limbs of Henle's loop, but its activity was very low and measurements were close to the sensitivity limit of the method. Both the absolute activity and the fraction of the total enzyme represented by Na-K-ATPase were severalfold higher than in kidney homogenates. Finally, the Na-K-ATPase activity measured in certain segments of the rat and rabbit nephron in this study seems sufficient to account in theory for the active component of the net sodium transport found in the corresponding region of the nephron with either in vivo or in vitro single tubule microperfusion techniques.

scholarly journals Two-Step Production of Neofructo-Oligosaccharides Using Immobilized Heterologous Aspergillus terreus 1F-Fructosyltransferase Expressed in Kluyveromyces lactis and Native Xanthophyllomyces dendrorhous G6-Fructosyltransferase

Catalysts ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 673 ◽  
Author(s):  
Burghardt ◽  
Baas ◽  
Gerlach ◽  
Czermak
Keyword(s):  
Response Surface Methodology ◽  
Enzyme Activity ◽  
Reaction Time ◽  
Aspergillus Terreus ◽  
Kluyveromyces Lactis ◽  
Xanthophyllomyces Dendrorhous ◽  
Initial Concentration ◽  
Total Enzyme Activity ◽  
Glycosidic Bonds ◽  
Total Enzyme

Fructo-oligosaccharides (FOS) are prebiotic low-calorie sweeteners that are synthesized by the transfer of fructose units from sucrose by enzymes known as fructosyltransferases. If these enzymes generate β-(2,6) glycosidic bonds, the resulting oligosaccharides belong to the neoseries (neoFOS). Here, we characterized the properties of three different fructosyltransferases using a design of experiments approach based on response surface methodology with a D-optimal design. The reaction time, pH, temperature, and substrate concentration were used as parameters to predict three responses: The total enzyme activity, the concentration of neoFOS and the neoFOS yield relative to the initial concentration of sucrose. We also conducted immobilization studies to establish a cascade reaction for neoFOS production with two different fructosyltransferases, achieving a total FOS yield of 47.02 ± 3.02%. The resulting FOS mixture included 53.07 ± 1.66 mM neonystose (neo-GF3) and 20.8 ± 1.91 mM neo-GF4.

scholarly journals EXTRACELLULAR COLD ACTIVE ENDOGLUCANASE AND PIGMENT PRODUCING PSYCHROTOLERANT PENICILLIUM PINOPHILUM

2016 ◽  
Vol 8 (10) ◽  
pp. 164 ◽  
Author(s):  
Abhas Kumar Maharana
Keyword(s):  
Sugarcane Bagasse ◽  
Endoglucanase Activity ◽  
Total Enzyme Activity ◽  
Cold Active Enzymes ◽  
Red Color ◽  
Cold Active ◽  
Penicillium Pinophilum ◽  
Groundnut Shell ◽  
Color Pigment ◽  
Total Enzyme

<p><strong>Objective: </strong>The objective of the present study was on <em>Penicillium pinophilum </em>strain F2 from soil samples of Jammu city having the potentiality to produce alkaline cold active endoglucanase and pigment.</p><p><strong>Methods: </strong><em>Penicillium pinophilum </em>strain F2,<em> </em>a<em> </em>psychrotolerant micro-fungus was isolated from soil of Jammu city, India by taking Czapek’s Dox agar incubated at 15 °C. The strain was screened for production of cold active enzymes by taking various substrates at 15 °C. Final production was done for cold active endoglucanase by using sugarcane bagasse and ground nut shell as substrates. Besides, the strain was also able to produce red color pigment at a low temperature which was further studied to optimize its production by changing pH and growth medium. The produced pigment was used for dyeing of wool and silk, and absorption percentages were also calculated.</p><p><strong>Results: </strong>Screening for the production of cold active enzymes revealed it as a good producer of cellulose followed by lipase and amylase. Endoglucanase production revealed the total enzyme titer (total enzyme activity) was found to be 5.032 folds higher in sugarcane bagasse (38.91 units) than groundnut shell (7.732 units). Endoglucanase activity was maximum 9.82±0.33 units/ml and 2.29±0.31 units/ml after 120 h of incubation at 15 °C by sugarcane bagasse and groundnut shells, respectively. Red color pigment production was maxima at pH 5 in Czapek’s Dox broth. Maximum absorption percentage was seen by the treatment soaked with mordant, i.e. 5% CuSO<sub>4 </sub>(51.52%) and without a mordant, it showed about 45.54%.</p><p><strong>Conclusion: </strong>Due to the above unique features and capability to produce cold active endoglucanase and pigment by strain F2, can be used significantly in various industries.</p>

scholarly journals The effects of starvation and experimental diabetes on phosphoenol-pyruvate carboxykinase in the guinea pig

1977 ◽  
Vol 164 (2) ◽  
pp. 357-361 ◽  
Author(s):  
K R F Elliott ◽  
C I Pogson
Keyword(s):  
Enzyme Activity ◽  
Guinea Pig ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Blood Glucose Concentration ◽  
Mitochondrial Fraction ◽  
Kidney Cortex ◽  
Total Enzyme Activity ◽  
The Mean ◽  
Mean Blood Glucose ◽  
Total Enzyme

1. Approx. 85% of liver phosphoenolpyruvate carboxykinase is associated with the mitochondrial fraction in the fed guinea pig. Enzyme activity is unchanged in diabetes, but doubles during starvation. In contrast with earlier reports, both cytoplasmic and mitochondrial activities were found to be increased. 2. In kidney cortex, total enzyme activity is increased in both starved and diabetic animals. These changes are associated with increases in the cytoplasmic activity alone. 3. In diabetic animals the mean blood-glucose concentration was 23.1 mM. Other blood metabolites were lower than those in the rat, and the animals did not show significant ketosis. 4. Changes in the rates of gluconeogenesis from lactate and propionate paralleled those in phosphoenolpyruvate carboxykinase activity.

Beta-adrenergic blockade and lipoprotein lipase activity in rat tissues after acute exercise

1991 ◽  
Vol 261 (4) ◽  
pp. R891-R897 ◽  
Author(s):  
A. Paulin ◽  
J. Lalonde ◽  
Y. Deshaies
Keyword(s):  
Lipoprotein Lipase ◽  
Acute Exercise ◽  
Vastus Lateralis ◽  
Vastus Lateralis Muscle ◽  
Rat Tissues ◽  
Adrenergic Blockade ◽  
Beta Adrenergic ◽  
Nonesterified Fatty Acids ◽  
Total Enzyme Activity ◽  
Total Enzyme

The present experiments were aimed at evaluating the acute effects of exercise on lipoprotein lipase (LPL) activity in untrained rats. The activity of LPL was measured in postheparin plasma (PHP) before and at various times after a 1-h run on a treadmill (22 m/min, O degrees grade). LPL in PHP was 50% below pre-exercise levels immediately and 3 h after the run but was increased 65% over resting levels 24 h postexercise. To further characterize the very early fall in LPL activity in response to exercise and to assess the possible involvement therein of the beta-adrenergic pathway, LPL in heart, vastus lateralis muscle (VLM), and white (WAT) and brown (BAT) adipose tissues was determined at rest and immediately after exercise in rats that were treated or not with nadolol (25 mg.kg-1.day-1 for 30 days). Immediately after 1 h of exercise, there was a reduction in total enzyme activity in WAT (40% below resting levels), BAT (-58%), VLM (-53%), and heart (-30%). Exercise reduced serum triacylglycerol levels (-64%) and doubled those of nonesterified fatty acids. beta-Adrenergic blockade did not affect any of these variables. Both exercise and nadolol lowered serum cholesterol levels by approximately 20%, but the effects were not additive. These results show that the global intravascular pool of LPL undergoes divergent, time-dependent alterations in response to a single bout of moderate exercise. The acute downregulation of postheparin plasma LPL immediately after exercise reflected a fall in the total enzyme pool of all tissues studied.(ABSTRACT TRUNCATED AT 250 WORDS)

Changes in mass and catalytic activity concentrations of aspartate aminotransferase isoenzymes in serum after a myocardial infarction.

1986 ◽  
Vol 32 (3) ◽  
pp. 496-500 ◽  
Author(s):  
A E Niblock ◽  
G Jablonsky ◽  
F Y Leung ◽  
A R Henderson
Keyword(s):  
Myocardial Infarction ◽  
Enzyme Activity ◽  
Catalytic Activity ◽  
Aspartate Aminotransferase ◽  
Left Ventricular ◽  
Peak Activity ◽  
Ventricular Failure ◽  
Total Enzyme Activity ◽  
Activity Concentrations ◽  
Total Enzyme

Abstract We used an RIA and inhibition of enzyme activity to monitor the changes in mass and catalytic concentrations of the aspartate aminotransferase (EC 2.6.1.1;AST) isoenzymes in serum after myocardial infarction. Cytosolic (c-AST) and mitochondrial (m-AST) forms of AST were present in sera from all 38 of our patients. Although the immunological and catalytic concentrations of both isoenzymes correlated well with the size of the infarct, c-AST gave a better measure than did m-AST. About 20% of the total enzyme activity at peak activity was from the mitochondrial isoenzyme. Both isoenzyme activities peak at very nearly the same time, but m-AST has the longer half-life. Immunological evidence of the mitochondrial isoenzyme can be detected in serum for at least eight days after the infarct. The presence of left ventricular failure produces greater serum isoenzyme activities than in those without failure.

scholarly journals PRESERVATION OF TOTAL, LYO-, AND DESMOENZYME ACTIVITY IN MAMMALIAN SALIVARY GLANDS FOLLOWING CHLORAL HYDRATE FORMALIN FIXATION

1964 ◽  
Vol 12 (9) ◽  
pp. 647-653 ◽  
Author(s):  
HOWARD H. CHAUNCEY ◽  
JOSEPH H. KRONMAN ◽  
MAYER A. LEVITT
Keyword(s):  
Acid Phosphatase ◽  
Salivary Glands ◽  
Chloral Hydrate ◽  
Animal Species ◽  
Insoluble Fraction ◽  
Nonspecific Esterase ◽  
Submandibular Salivary Glands ◽  
High Level ◽  
Cryostat Sections ◽  
Total Enzyme

Acid phosphatase, alkaline phosphatase, nonspecific esterase, pseudocholinesterase, leucine aminopeptidase, and β-d-galactosidase activities of parotid and submandibular salivary glands were evaluated in six animal species. Assays for total enzyme, lyoenzyme, and demoenzyme were performed on unfixed and chloral hydrate formalin (CHF) fixed frozen cryostat sections. Following fixation lyoenzyme (soluble fraction) activity exhibited extreme reduction for all enzymes except pseudocholinesterase, while the demoenzyme (insoluble fraction) activity of acid phosphatase, nonspecific esterase, pseudocholinesterase, and β-d-galactosidase was maintained at a high level or increased. Since removal of lyoenzyme activity and retention of desmoenzyme activity are requisites in histochemical localization, this fixative may be the preferred method for handling tissues prior to the localization of the above cited enzymes. Several hypotheses are proposed to explain the increased desmoenzyme (nonspecific esterase and β-d-galactosidase) noted subsequent to fixation.

Estimates of the Zinc Requirements of Marine Organisms

1969 ◽  
Vol 26 (1) ◽  
pp. 145-150 ◽  
Author(s):  
John E. Pequegnat ◽  
Scott W. Fowler ◽  
Lawrence F. Small
Keyword(s):  
Marine Environment ◽  
Marine Organisms ◽  
Minimum Potential ◽  
Total Enzyme

The amount of enzyme-bound zinc is calculated from estimates of total enzyme concentrations and the number of zinc atoms per mole of these enzymes. This estimate is shown to be smaller than measured concentrations in marine organisms, indicating that zinc is accumulated in excess of the organisms' immediate needs. A minimum "potential fertility" for zinc is calculated; the results indicate that zinc is not limiting in the marine environment.

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