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W Lipp

Publications and source records attributed to W Lipp.

15 recordsLinked to original sources
PubMed1986

[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium].

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.

Animals↗
PubMed1985

[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium].

In porcine areolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the enzyme activities remained almost unchanged during the period of investigation. Of the dehydrogenases, the diaphorases as well as succinate and lactate dehydrogenase demonstrated generally an intensive activity within the epithelia. The activity of the other dehydrogenases was only low. The activity of unspecific esterase was very intensive within the uterine epithelia but remarkably low within chorionic epithelia. Contrarily, the reaction of adenosine triphosphatase was more intensive within chorionic than uterine epithelia. All investigated glucosidases reacted distinctly positive within chorionic epithelia, but only beta-N-acetyl-hexosaminidase and beta-galactosidase in uterine epithelia. The high activity of acid phosphatase, especially within the chorionic epithelium, seems to be connected with uteroferrin, an iron-binding protein. The histochemical results are discussed in context with the function of the areolae in histiotrophic nutrition and iron transport.

Animals↗
PubMed1979

[Histological localization of hydrolases in the epididymis of the dog].

Localization and activity of five hydrolases (alkaline phosphatase, adenosine triphosphatase, acid phosphatase, nonspecific esterase and leucylamino-peptidase) were evaluated histochemically in the epididymides of mature dogs. In the ductuli efferentes, cilia and apical parts of the epithelial cells displayed high activity of alkaline phosphatase and adenosine triphosphatase. Strong activity of acid phosphatase, nonspecific esterase and leucylamino-peptidase was present in the basal and supranuclear zones of the epithelium of the ductuli efferentes. Stereocilia of all three segments of the ductus epididymidis showed a high activity of alkaline phosphatase. Positive adenosine triphosphatase reaction was confined to the stereocilia of the initial segment. A complex pattern of acid phosphatase activity was observed in the middle segment. The subdivision of the middle segment in four subsegments was therefore suggested. In the epithelium of the initial segment only a few nonspecific esterase-positive cells were seen. The infranuclear and basal areas of the epithelium in the middle segment and the supranuclear zone of the terminal segment displayed distinct nonspecific esterase activity. The possible contribution of the hydrolases to the function of the epididymis is discussed.

Acid Phosphatase↗
PubMed1979

[Enzyme histochemical studies on the epithelium of the epididymis of the tomcat (author's transl)].

The histochemical localization of some oxidoreductases was investigated in the epididymides of adult tomcats. Succinate dehydrogenase, lactate dehydrogenase, beta-hydroxybutyrate-dehydrogenase revealed their highest activity in corpus and cauda epididymidis whereas glucose-6-phosphate-dehydrogenase was strongest in the caput. The activity of the diaphorases and of cytochrome oxidase in the epididymal epithelium increased from caput towards the cauda epididymidis. The reaction for isocitrate dehydrogenase was distinct throughout the whole length of the ductus epididymidis. Our findings were compared with the biochemical results of other authors and the functions of the oxidoreductases in the epididymal epithelium were briefly discussed.

Animals↗
PubMed1978

[Histotopography of glycosidases in the accessory glands of the boar before and after castration].

The histochemical distribution of six glycosidases (N-acetyl-beta-glucosaminidase, beta-galactosidase, beta-glucuronidase, alpha-galactosidase, alpha-mannosidase and alpha-fucosidase) was investigated in the prostate, glandula vesicularis and glandula bulbourethralis of castrated and non-castrated adult boars. The functions of the glycosidases in the male accessory sex glands of the boar and their androgen dependence are discussed briefly.

Animals↗
PubMed1978

[Histotopics of lysosomal enzymes in the epididymis of the tom-cat (author's transl)].

The histochemical localization of 6 lysosomal enzymes was studied in the epididymis of adult tomcats. A weak to distinct reaction for acid phosphatase, leucyl-amino-peptidase and non--specific esterase could be observed in the epithelium of the ductus epididymidis in all three segments. Among the glycosidases, N-acetyl-beta-glucosaminidase displayed the strongest activity. alpha-man and alpha-fuc could not be demonstrated. For N-Acetyl-beta-glucosaminidase, beta-Galactosidase, acid phosphatase and non-specific esterase, an increase of enzyme activity from the initial segment towards the terminal segment was seen. Intracellularly, the maximum of enzyme activity of those four enzymes was supranuclear. This histochemically enstablished pattern of enzyme activity in the epididymis of the tomcat was compared with those of other mammals. The possible functions of enzymes in the epididymis was briefly discussed.

Acid Phosphatase↗
PubMed1976

[Histotopics of glycosidases in the accessory sex glands of bull (author's transl)].

The histochemical distribution of 4 glycosidases (alpha-Mannosidase, beta-Glucuronidase, N-Acetyl-beta-glucosaminidase and beta-Galactosidase) has been studied in the accessory sex glands of bulls. All glcosidases displayed the highest activity in the distal part of the caput epididymidis and in the cauda epididymidis. A distinct activity of N-Acetyl-beta-glucosaminidase and beta-galactosidase was observed in the seminal vesicle, the ampulla ductus deferentis and in the prostatic gland. In the epithelium of the bulbourethral gland only a weak content of beta-Galactosidase could be demonstrated histochemically. The functional role of the glycosidases in the accessory sex organs is discussed briefly.

Acetylglucosaminidase↗