HYDROLYSIS OF GLYCEROLPHOSPHATIDES BY PLASTID PHOSPHATIDASE C

1956 ◽  
Vol 34 (1) ◽  
pp. 967-980 ◽  
Author(s):  
Morris Kates
Keyword(s):  
Ethyl Ether ◽  
Phosphatidyl Choline ◽  
Phosphatidyl Ethanolamine ◽  
Enzymatic Reaction ◽  
Phosphatidyl Serine ◽  
Ph Optimum ◽  
Soybean Phosphatide ◽  
Optimum Ph ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

Studies of the influence of structural variation in the glycerolphosphatide molecule on the hydrolysis of this class of compounds by plastid phosphatidase C showed that the presence of both fatty acid ester groups is necessary for enzymatic reaction; that release of nitrogenous bases occurred, in the presence of ethyl ether, from phosphatidyl cholines, phosphatidyl ethanolamine, and phosphatidyl serine; and that a phosphatidyl choline was hydrolyzed more rapidly than the corresponding phosphatidyl ethanolamine or phosphatidyl serine. The rate of hydrolysis of phosphatidyl choline was influenced greatly by the chain length and degree of unsaturation of the fatty acids. The corresponding phosphatidic acid formed in the hydrolysis of (dipalmitoyl)- or (dipalmitoleyl)-lecithin by carrot phosphatidase C was isolated. Studies on the hydrolysis of crude soybean phosphatide by phosphatidase C showed that both choline and ethanolamine were liberated in the absence of ethyl ether, at an optimum pH of 4.8; in the presence of ether, the rate of liberation of each base was increased, and the pH optimum was between 4.8 and 6. Soybean phosphatide probably contains a substance that stimulates the enzymatic hydrolysis.

HYDROLYSIS OF GLYCEROLPHOSPHATIDES BY PLASTID PHOSPHATIDASE C

1956 ◽  
Vol 34 (5) ◽  
pp. 967-980 ◽  
Author(s):  
Morris Kates
Keyword(s):  
Ethyl Ether ◽  
Phosphatidyl Choline ◽  
Phosphatidyl Ethanolamine ◽  
Enzymatic Reaction ◽  
Phosphatidyl Serine ◽  
Ph Optimum ◽  
Soybean Phosphatide ◽  
Optimum Ph ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

Studies of the influence of structural variation in the glycerolphosphatide molecule on the hydrolysis of this class of compounds by plastid phosphatidase C showed that the presence of both fatty acid ester groups is necessary for enzymatic reaction; that release of nitrogenous bases occurred, in the presence of ethyl ether, from phosphatidyl cholines, phosphatidyl ethanolamine, and phosphatidyl serine; and that a phosphatidyl choline was hydrolyzed more rapidly than the corresponding phosphatidyl ethanolamine or phosphatidyl serine. The rate of hydrolysis of phosphatidyl choline was influenced greatly by the chain length and degree of unsaturation of the fatty acids. The corresponding phosphatidic acid formed in the hydrolysis of (dipalmitoyl)- or (dipalmitoleyl)-lecithin by carrot phosphatidase C was isolated. Studies on the hydrolysis of crude soybean phosphatide by phosphatidase C showed that both choline and ethanolamine were liberated in the absence of ethyl ether, at an optimum pH of 4.8; in the presence of ether, the rate of liberation of each base was increased, and the pH optimum was between 4.8 and 6. Soybean phosphatide probably contains a substance that stimulates the enzymatic hydrolysis.

Polarographic study of hydrolysis of [8-lysine]vasopressin and its derivatives with blood serum of pregnant women

1980 ◽  
Vol 45 (4) ◽  
pp. 1099-1108 ◽  
Author(s):  
Mikuláš Chavko ◽  
Michal Bartík ◽  
Evžen Kasafírek
Keyword(s):  
Blood Serum ◽  
Pregnant Women ◽  
Degree Of Hydrolysis ◽  
Polarographic Study ◽  
Ph Optimum ◽  
Lysine Vasopressin ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Vasopressin Analogues

A polarographic study of the hydrolysis of [8-lysine]vasopressin and some hormonogens of the vasopressin series with the blood serum of women in the last week of pregnancy was studied. The dependence of hydrolysis on pH (pH optimum: 7.4-7.50, substrate concentration (Km 1.2 . 10-5M), pH stability and thermal stability were determined. The rate of hydrolysis of individual vasopressin analogues decreases in the order: [8-lysine]vasopressin > Nα-glycyl-prolyl[8-lysine]-vasopressin > Nα-leucyl-[8-lysine]vasopressin > Nα-alanyl-[8-lysine]vasopressin > Nα-phenyl alanyl-[8-lysine]vasopressin > Nα-diglycyl-[8-lysine]vasopressin > Nα-prolyl-[8-lysine]vasopressin > Nα-triglycyl-[8-lysine]vasopressin > Nα-sarcosyl-glycyl-[8-lysine]vasopressin. The degree of hydrolysis gradually increases to a multiple with the length of the pregnancy in consequence of the presence of oxytocine. However, vasopressin is also hydrolysed to a small extent with the enzymes from the blood sera of non-pregnant women. Under similar analytical conditions oxytocin was not hydrolysed with the sera of non-pregnant women and therefore oxytocin is a more suitable substrate than vasopressin for polarographic determination of serum oxytocinase.

428. The acid phosphatase of mammary tissue of the cow and the rat

1950 ◽  
Vol 17 (3) ◽  
pp. 306-311 ◽  
Author(s):  
J. E. C. Mullen
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Replacement Therapy ◽  
Marked Effect ◽  
Mammary Tissue ◽  
Optimum Ph ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

1. Mammary tissue of the cow and the rat contains acid phosphatase. The respective pH optima are 5·5–5·8 and 6·0.2. The enzyme in cow mammary tissue is probably one of type AII in the Folley & Kay (10) classification.3. The acid phosphatase of cow mammary tissue is inhibited by a factor in raw cows' milk. This factor is destroyed by heat.4. On the basis of rate of hydrolysis of phenylphosphate at the optimum pH there is about 5 times more alkaline phosphatase in the mammary tissue of the cow than acid phosphatase.5. The effect of adrenalectomy and replacement therapy through the administration of cortical steroids has no marked effect on the acid phosphatase of rat mammary tissue.

ACID PHOSPHATASE HYDROLYSIS OF PHOSPHORIC ESTERS

1955 ◽  
Vol 33 (1) ◽  
pp. 539-544 ◽  
Author(s):  
G. E. Delory ◽  
G. S. Wiberg ◽  
Merle Hetherington
Keyword(s):  
Acid Phosphatase ◽  
Seminal Fluid ◽  
Optimum Ph ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

The rate of hydrolysis and optimum pH of hydrolysis of seminal fluid acid phosphatase have been studied for a number of phosphoric esters. As the acidity of the substrate increases there is a tendency for the rate of hydrolysis to increase and for the optimum pH to move farther away from neutrality. The increased rate of hydrolysis of phenol phosphates or of substituted phenol phosphates can not be accounted for by phenolase activity.

The phospholipids of Hansenula wingei, mating type 21

1972 ◽  
Vol 18 (10) ◽  
pp. 1569-1573
Author(s):  
J. C. Wirth ◽  
A. R. Magliulo
Keyword(s):  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Phosphatidyl Choline ◽  
Phosphatidyl Ethanolamine ◽  
Deae Cellulose ◽  
Phosphatidyl Serine ◽  
Hansenula Wingei ◽  
Layer Chromatography ◽  
Cellulose Column ◽  
Choline Phosphatidyl

The phospholipid fraction of the yeast H. wingei was studied by a combination of DEAE-cellulose column chromatography and thin-layer chromatography. Phosphatidyl choline, phosphatidyl serine, and phosphatidyl ethanolamine were identified. The absence of phosphoinositide was noted. An unknown acidic phospholipid accounts for less than 1% of the total phosphorus. A cerebroside or cerebroside-like compound was provisionally identified.

scholarly journals Identification and Characterization of Bacterial Lipase from Plateu Soil in West Java

2017 ◽  
Vol 18 (02) ◽  
pp. 103-108
Author(s):  
Vivitri Dewi Prasasty ◽  
Vinella Winata ◽  
Muhammad Hanafi
Keyword(s):  
Heat Stability ◽  
Industrial Applications ◽  
West Java ◽  
Ph Optimum ◽  
Good Efficiency ◽  
Optimum Ph ◽  
Glycerol Ester ◽  
Lipase Screening ◽  
Hydrolysis Of

Lipases are known as glycerol ester hydrolases that catalyze the hydrolysis of triglycerides into free fatty acids and glycerol. Lipases are found in human, animal, plant, and microorganisms. The aim of this research is to identify lipase producers and characterize bacterial lipase from West Java plateau soil. Plateau soil bacteria samples were isolated on lipase screening medium containing Rhodamine B. Olive oil was used as a substrate in screening and production medium bacterial lipases. From 16 bacterial isolate of lipase producers, 14 were identified as Bacillus sp. and the others were identified as Pseudomonas alcaligenes. All isolates were taken into production step to determine their lipase activities. Moreover, top 3 lipase activities out of 16 lipase activities were chosen to find the optimum pH and temperature. Both characterizations showed pH optimum and temperature optimum from each lipase. These optimum condition were used in heat stability characterization for each lipase samples. The result showed that lipase from isolate COK 2 in optimum pH 4 and temperature 50oC was the most stable lipase due to this sample has good and stable activity for 1 to 5 hours incubation time. Lipase sample from isolate COK 2 has good efficiency for lipase productivity in acid condition and high temperature. Results of this investigation could encourage utilization of these activity enhancers for various industrial applications.

THE LIVER PHOSPHOLIPIDS OF THE DEVELOPING CHICK EMBRYO

1967 ◽  
Vol 45 (5) ◽  
pp. 627-639 ◽  
Author(s):  
R. C. Noble ◽  
J. H. Moore
Keyword(s):  
Fatty Acid ◽  
Phosphatidyl Choline ◽  
Phosphatidyl Ethanolamine ◽  
Phosphatidyl Serine ◽  
Chick Embryos ◽  
Ethanolamine Phosphatidyl ◽  
The Individual ◽  
Docosahexaenoic Acids ◽  
Choline Phosphatidyl ◽  
Fatty Acid Compositions

The concentrations and fatty acid compositions of the individual phospholipids in the livers of chick embryos on the 13th, 15th, 17th, 19th, and 21st days of incubation were compared with the concentrations and fatty acid compositions of the individual yolk phospholipids. The liver phospholipids contained higher proportions of phosphatidyl ethanolamine, phosphatidyl serine, and diphosphatidyl glycerol, and lower proportions of phosphatidyl choline, than did the yolk phospholipids. There was a constant increment (0.96 mg/day) of phosphatidyl choline in the liver during the period of incubation studied. The phosphatidyl choline, phosphatidyl ethanolamine, and phosphatidyl serine of the liver generally contained higher concentrations of stearic, arachidonic, and docosahexaenoic acids, and lower concentrations of palmitic and oleic acids than did these phospholipid fractions in the yolk. The fatty acid compositions of the sphingomyelin in the liver and yolk were similar. The most pronounced changes in the fatty acid composition of the liver phospholipids during embryonic development were observed in the phosphatidyl choline fraction. These changes suggested that the α-palmitoyl-β-arachidonyl phosphatidyl choline in the liver was gradually replaced by α-stearoyl-β-linoleoyl phosphatidyl choline and a-stearoyl-β-docosahexaenoyl phosphatidyl choline.

Lipids of Cod Muscle and the Effect of Frozen Storage

1966 ◽  
Vol 23 (7) ◽  
pp. 1025-1036 ◽  
Author(s):  
E. G. Bligh ◽  
Margaret A. Scott
Keyword(s):  
Total Lipid ◽  
Phosphatidyl Choline ◽  
Gadus Morhua ◽  
Phosphatidyl Ethanolamine ◽  
Fatty Acid Content ◽  
Frozen Storage ◽  
Phospholipid Content ◽  
Silicic Acid Chromatography ◽  
Significant Difference ◽  
Hydrolysis Of

The lipid composition of fresh and frozen cod (Gadus morhua) muscle was studied using silicic acid chromatography. Dark cod muscle contained about three times as much total lipid as white muscle but the composition was quite similar. The most significant difference was that the dark tissue lipid contained more esterified cholesterol and less phosphatidyl choline. Frozen storage for up to 9 months at −12 C showed that the free fatty acid content increased from 5 to 326 mg/100 g tissue due to the hydrolysis of phosphatidyl ethanolamine and phosphatidyl choline. Other phospholipids were not hydrolyzed. Phosphatidyl ethanolamine hydrolysis ceased after storage for 4 months, whereas hydrolysis of phosphatidyl choline continued thereafter at a slower rate. After 9 months, the phospholipid content of the total lipid had dropped from 84 to 32% and only 13% of the original phosphatidyl ethanolamine and phosphatidyl choline remained unhydrolyzed.

scholarly journals Glyceride lipases in nerve endings of guinea-pig brain and their stimulation by noradrenaline, 5-hydroxytryptamine and adrenaline

1973 ◽  
Vol 132 (2) ◽  
pp. 233-248 ◽  
Author(s):  
O. S. Vyvoda ◽  
C. E. Rowe
Keyword(s):  
Guinea Pig ◽  
Synaptic Vesicles ◽  
Protein Concentration ◽  
Synaptic Membranes ◽  
Ph Optimum ◽  
Triglyceride Lipase ◽  
Monoglyceride Lipase ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Guinea Pig Brain

1. Combined guinea-pig cortex and cerebellum was shown to contain triglyceride lipase, diglyceride lipase and monoglyceride lipase, which were assayed by the release of [1-14C]palmitate from [1-14C]palmitoylglycerol esters. Triglyceride lipase and diglyceride lipase were found in all particulate fractions. 2. With osmotically ruptured synaptosomes the rates of release of palmitate from glyceryl tripalmitate and glyceryl dipalmitate were 7–25μmol/h per g of protein and 0.18–0.69mmol/h per g of protein respectively. The logarithm of the rate of hydrolysis of glyceryl monopalmitate increased linearly with the logarithm of protein concentration. The pH optima of triglyceride lipase and diglyceride lipase were between 7 and 8. The pH optimum for monoglyceride lipase was approx. 8. 3. Triglyceride lipase and diglyceride lipase of osmotically ruptured synaptosomes were stimulated by noradrenaline, 5-hydroxytryptamine and adrenaline. Triglyceride lipase of isolated synaptic membranes was stimulated by 0.01–1mm-noradrenaline. Aging of membranes at 0°C decreased activity, which could still be stimulated by noradrenaline. Diglyceride lipase of isolated membranes was stimulated by 1μm–1mm-noradrenaline. The activity of triglyceride lipase in isolated synaptic vesicles was diminished by 1mm-5-hydroxytryptamine.

Sign in / Sign up

Export Citation Format

Share Document