Improved Synthetic Methods of Firefly Luciferin Derivatives for Use in Bioluminescent Analysis of Hydrolytic Enzymes; Carboxylic Esterase and Alkaline Phosphatase

1992 ◽  
Vol 65 (10) ◽  
pp. 2604-2610 ◽  
Author(s):  
Yoshiaki Toya ◽  
Masaharu Takagi ◽  
Tadao Kondo ◽  
Hisao Nakata ◽  
Minoru Isobe ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Hydrolytic Enzymes ◽  
Synthetic Methods ◽  
Firefly Luciferin ◽  
Bioluminescent Analysis

ENZYMIC CHANGES IN THE CERVIX OF THE RAT AND HAMSTER DURING THE OESTROUS CYCLE AND THE EFFECT OF STEROIDS

1977 ◽  
Vol 72 (2) ◽  
pp. 153-161 ◽  
Author(s):  
ELIZABETH ZACHARIAH ◽  
N. R. MOUDGAL
Keyword(s):  
Alkaline Phosphatase ◽  
Specific Activity ◽  
Protein Biosynthesis ◽  
Hydrolytic Enzymes ◽  
Maximal Activity ◽  
Inhibitory Effect ◽  
Oestrous Cycle ◽  
Single Subcutaneous Injection ◽  
Arylsulphatase A ◽  
Phosphatase Alkaline

SUMMARY Changes in four hydrolytic enzymes, namely acid phosphatase, alkaline phosphatase, arylsulphatase A and B, of the cervix of the rat and hamster have been studied during the 4-day oestrous cycle. All four enzymes showed maximal activity on the day of oestrus and least activity on day 2 of dioestrus. All the enzymes showed significant reduction of activity after ovariectomy, arylsulphatase A and B showing the earliest changes in specific activity. A single subcutaneous injection of 0·02 μg oestradiol-17β/rat increased the specific activity of arylsulphatase A and B from the low ovariectomized level to that observed in control oestrous animals within 18 and 6 h respectively. A higher concentration of oestradiol-17β (2·0 μg) had an inhibitory effect. Progesterone was without effect on arylsulphatase B activity, but when given (2·0 mg) with 0·02 μg oestradiol-17β, it inhibited the response to oestrogen. Cycloheximide prevented the rise in arylsulphatase B activity occurring after oestrogen injection, suggesting a regulation of cervical arylsulphatase B at the level of protein biosynthesis. These results suggest that arylsulphatase B activity may be induced by oestrogen in the cervix of the rat.

scholarly journals The tegument ofSchistosoma mansoni: a histochemical investigation

Parasitology ◽  
1976 ◽  
Vol 72 (1) ◽  
pp. 99-109 ◽  
Author(s):  
P. R. Wheater ◽  
R. A. Wilson
Keyword(s):  
Alkaline Phosphatase ◽  
Adenosine Triphosphatase ◽  
Hydrolytic Enzymes ◽  
Mitochondrial Enzymes ◽  
Biosynthetic Activity ◽  
Histochemical Investigation ◽  
Enzyme Content ◽  
Dorsal Tegument ◽  
Main Components

The main components of the schistosome tegument were found to be neutral glycoprotein and phospholipid; a small quantity of glycolipid was observed in the male dorsal tegument. The tegument can be differentiated from other schistosome tissues on the basis of enzyme content; three hydrolytic enzymes were shown to be specifically localized in the tegument: alkaline phosphatase, adenosine triphosphatase and indoxyl esterase. It is suggested that these enzymes could be used as intrinsic markers for tegument structures. The subtegumental cells appear to be the major sites of biosynthetic activity since they contain large amounts of RNA and mitochondrial enzymes.

scholarly journals THE ACTIVITY OF HYDROLYTIC ENZYMES IN DIFFERENT LIFE STAGES OF THE HOUSE FLY MUSCA DOMESTICA L.

2019 ◽  
pp. 589-593
Author(s):  
Silivanova ◽  
Levchenko
Keyword(s):  
Alkaline Phosphatase ◽  
Life Cycle ◽  
Phosphatase Activity ◽  
Enzyme Activities ◽  
Hydrolytic Enzymes ◽  
Pupal Stage ◽  
House Fly ◽  
Detoxification Enzymes ◽  
Life Stages ◽  
Metabolic Resistance

The problem of insect resistance to insecticides attracts great attention in the world. It is known that metabolic resistance in insects is provided by the activity of detoxi-fication enzymes, including hydrolases. Enzyme activities do not remain the same during the life cycle of insects. The purpose of this study was to assess the activity of acetylcholinesterase, alkaline and acid phosphatases in the house fly Musca domes-tica L. at the different lifestages. Enzyme activities were determined in homogenates obtained from eggs, larvae of II – III instar, pupae, and adults (1, 5, and 10 days old) of the M. domestica laboratory strain. According to the obtained results, the acid phosphatase activity did not differ in different life stages of M. domestica, and the activity of acetylcholinesterase and alkaline phosphatase varied in ontogenesis. Alkaline phosphatase activity was minimal in the eggs, increased in the larvae, and decreased again at the pupal stage. The activity of acetylcholinesterase was minimal in the eggs as well and increased with the M. domestica development up to the pupal stage. The acetylcholinesterase activity in one-day-old adults was similar to that in pupal stage.The revealed features of the activity of hydrolytic detoxification enzymes at different life cycle stages of the M. domestica might determine the characteristics of metabolic resistance to insecticides, which, in our opinion, should be taken into account when one studies of insecticide resistance in house flies.

scholarly journals DIFFERENCES IN ENZYME CONTENT OF AZUROPHIL AND SPECIFIC GRANULES OF POLYMORPHONUCLEAR LEUKOCYTES

1968 ◽  
Vol 39 (2) ◽  
pp. 286-298 ◽  
Author(s):  
Dorothy Ford Bainton ◽  
Marilyn G. Farquhar
Keyword(s):  
Alkaline Phosphatase ◽  
Polymorphonuclear Leukocytes ◽  
Basic Protein ◽  
Developmental Stages ◽  
Hydrolytic Enzymes ◽  
Enzyme Content ◽  
Specific Granules ◽  
Rabbit Bone ◽  
Thiolacetic Acid ◽  
Enzyme Alkaline Phosphatase

Histochemical procedures for PMN granule enzymes were carried out on smears prepared from normal rabbit bone marrow, and the smears were examined by light microscopy. For each of the enzymes tested, azo dye and heavy metal techniques were utilized when possible. The distribution and intensity of each reaction were compared to the distribution of azurophil and specific granules in developing PMN. The distribution of peroxidase and six lysosomal enzymes (acid phosphatase, arylsulfatase, ß-galactosidase, ß-glucuronidase, esterase, and 5'-nucleotidase) corresponded to that of azurophil granules. Progranulocytes contained numerous reactive granules, and later stages contained only a few. The distribution of one enzyme, alkaline phosphatase, corresponded to that of specific granules. Reaction product first appeared in myelocytes, and later stages contained numerous reactive granules. The results of tests for lipase and thiolacetic acid esterase were negative at all developmental stages. Both types of granules stained for basic protein and arginine. It is concluded that azurophil and specific granules differ in their enzyme content. Moreover, a given enzyme appears to be restricted to one of the granules. The findings further indicate that azurophil granules are primary lysosomes, since they contain numerous lysosomal, hydrolytic enzymes, but the nature of specific granules is uncertain since, except for alkaline phosphatase, their contents remain unknown.

scholarly journals Cytochemical localization of certain hydrolytic enzymes at various stages of development of Achlya flagellata mycelium

2015 ◽  
Vol 41 (2) ◽  
pp. 265-282 ◽  
Author(s):  
I. Palczewska ◽  
G. Jagodzka
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Azo Dyes ◽  
Acid Phosphatase Activity ◽  
Hydrolytic Enzymes ◽  
Cytochemical Localization ◽  
Cytoplasmic Granules ◽  
End Products ◽  
E 600 ◽  
Phosphatase Alkaline

The standard coupling azo dyes techniques were used to reveal the activities of acid phosphatase, alkaline phosphatase, esterase and β-galactoidase in the vegetative and reproductive cycle of <i>Achlya flagellata</i>. The end-products of the enzymic reactions, with the exception of E 600 sentisive esterese, which is localized in cytoplasm, occured in cytoplasmic granules. These granules are expected to be spherosomes. Acid phosphatase activity is high in differentiating sporangia, in antheridial hyphae and in degenerating oospheres where hydrolytic processes occur. β-galactosidase is the least active enzyme in the mycelium of <i>Achlya</i>.

The tegument ofSchistosoma mansoni:a histochemical investigation

Parasitology ◽  
1976 ◽  
Vol 72 (1) ◽  
pp. 99-109 ◽  
Author(s):  
P. R. Wheater ◽  
R. A. Wilson
Keyword(s):  
Alkaline Phosphatase ◽  
Adenosine Triphosphatase ◽  
Hydrolytic Enzymes ◽  
Mitochondrial Enzymes ◽  
Biosynthetic Activity ◽  
Histochemical Investigation ◽  
Enzyme Content ◽  
Dorsal Tegument ◽  
Main Components

SummaryThe main components of the schistosome tegument were found to be neutral glycoprotein and phospholipid; a small quantity of glycolipid was observed in the male dorsal tegument. The tegument can be differentiated from other schistosome tissues on the basis of enzyme content; three hydrolytic enzymes were shown to be specifically localized in the tegument: alkaline phosphatase, adenosine triphosphatase and indoxyl esterase. It is suggested that these enzymes could be used as intrinsic markers for tegument structures. The subtegumental cells appear to be the major sites of biosynthetic activity since they contain large amounts of RNA and mitochondrial enzymes.

UTERINE AND PLACENTAL ENZYMES

1964 ◽  
Vol 46 (2) ◽  
pp. 217-229 ◽  
Author(s):  
E. S. E. Hafez
Keyword(s):  
Alkaline Phosphatase ◽  
Reproductive Cycle ◽  
Reproductive Tract ◽  
Enzyme System ◽  
Succinic Dehydrogenase ◽  
Hydrolytic Enzymes ◽  
Carbonic Anhydrase Activity ◽  
Gonadal Hormones ◽  
Female Reproductive Tract ◽  
Species Specific

ABSTRACT The effects of ovariectomy and exogenous gonadal hormones on uterine enzymes have been examined for several laboratory mammals. Qualitative and quantitative measurement of uterine and placental enzymes involve histochemical, cytochemical and biochemical techniques. Enzymes have a wide and characteristic distribution in the female reproductive tract. The pattern of distribution varies showing peculiar species – specific differences in the anatomical localization of the enzyme and its relationship to the reproductive cycle. Progestational responses involve major endometrial growth and striking change in the enzyme system. The amount and biochemical composition of endometrial secretions vary with the stage of reproductive cycle. The placenta contains a complex enzyme system which has been classified into five major groups: hydrases, transferases, oxidoreductases, lyases and isomerases. The passage of many substances across the placental barrier is chemically regulated; the cytoplasm of barrier contains several enzymes and organelles. Carbonic anhydrase activity of the endometrium increases markedly during the luteal phase of the cycle and during pregnancy in the rabbit but not in some other species. Alkaline phosphatase is widely distributed in all types of placenta, in maximal concentration in species producing no fructose. Several hydrolytic enzymes are associated with the small cytoplasmic particles, the lysosomes, β-glucuronidase of the endometrial and glandular epithelia shows cyclical changes with the oestrus cycle. The activity of the succinic dehydrogenase may be an index of the functional status of the epithelial cells. Some enzymes e. g. acid and alkaline phosphatase, 5-nucleotidase and adenosinetriphosphate show a typical »secretion cycle«. The role of certain uterine enzymes in implantation of blastocyst deserves investigation.

scholarly journals Further Studies on the Lyo and Desmo Components of Several Hydrolytic Enzymes and Their Histochemical Significance

1959 ◽  
Vol 5 (2) ◽  
pp. 279-288 ◽  
Author(s):  
Mark J. Hannibal ◽  
Marvin M. Nachlas
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Aqueous Medium ◽  
Incubation Medium ◽  
Leucine Aminopeptidase ◽  
Hydrolytic Enzymes ◽  
Striking Similarity ◽  
Tissue Sections ◽  
And Diffusion

This report describes additional studies of the lyo and desmo components of esterase, alkaline phosphatase, acid phosphatase, leucine aminopeptidase, and ß-glucuronidase. The techniques used have already been reported (7). Enzyme diffusion occurs to different degrees in different fixatives, and varies somewhat with each enzyme. Loss of enzymatic activity during fixation occurs as a result of both inactivation due to the chemical reaction of the fixative with the enzymic protein, and diffusion of the lyo component into the fixative. The amount of diffusion into formalin can be reduced by the addition of salts, sucrose, or methocel. The pH of the aqueous medium significantly influences the removal of the lyo fraction from the tissue section. A striking similarity can be noted in the proportions of each fraction of enzyme present in the kidney of the rat, dog, and man. The procedure of fixation and paraffin embedding of tissue blocks does not wholly prevent the diffusion of the lyo component from the tissue sections when they are subsequently immersed in the aqueous incubation medium.

Activités des hydrolases rénales au cours du développement pré- et post-natal de la souris

1985 ◽  
Vol 63 (6) ◽  
pp. 731-734 ◽  
Author(s):  
C. Niederst ◽  
M. Dauça
Keyword(s):  
Alkaline Phosphatase ◽  
Developmental Stage ◽  
Activity Patterns ◽  
Hydrolytic Enzymes ◽  
Suckling Period ◽  
Gamma Glutamyltransferase ◽  
Trehalase Activity ◽  
Maltase Activity

The fetal and postnatal activity patterns of different hydrolytic enzymes (alkaline phosphatase, gamma-glutamyltransferase, trehalase, maltase, glucoamylase, lactase, and sucrase) have been examined in mouse renal homogenates. Alkaline phosphatase and gamma-glutamyltransferase activities presented approximately similar changes. They increased from 18 days of gestation up to 30 days after birth. These activities showed marked increases during the 3rd and 4th postnatal weeks. A similar important rise was observed for trehalase activity at the end of the suckling period. Maltase activity increased gradually after birth. Traces of lactase, sucrase, and glucoamylase activities were detected at each developmental stage.

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