Testicular involution after optic enucleation: Ultrastructure and alkaline phosphatase cytochemistry of the peritubular tissue

1978 ◽  
Vol 151 (2) ◽  
pp. 213-225 ◽  
Author(s):  
Curtis J. Gravis
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Cytochemistry ◽  
Peritubular Tissue

Asparagine-linked carbohydrate does not determine the cellular location of yeast vacuolar nonspecific alkaline phosphatase

1982 ◽  
Vol 152 (2) ◽  
pp. 865-873
Author(s):  
D W Clark ◽  
J S Tkacz ◽  
J O Lampen
Keyword(s):  
Electron Microscopy ◽  
Alkaline Phosphatase ◽  
Subcellular Fractionation ◽  
Carbohydrate Moiety ◽  
Specific Alkaline Phosphatase ◽  
Cellular Location ◽  
Nitrophenyl Phosphate ◽  
Phosphatase Cytochemistry

The nonspecific alkaline phosphatase of Saccharomyces sp. strain 1710 has been shown by phosphatase cytochemistry to be exclusively located in the vacuole, para-Nitrophenyl phosphate-specific alkaline phosphatase is not detected by this procedure because the activity of this enzyme is sensitive to the fixative agent, glutaraldehyde. To determine whether the oligosaccharide of nonspecific alkaline phosphatase is necessary to transport the enzyme into the vacuole, protoplasts were derepressed in the absence or in the presence of tunicamycin, an antibiotic which interferes with the glycosylation of asparagine residues in proteins. The location of the enzyme in the tunicamycin-treated protoplasts, as determined by electron microscopy and subcellular fractionation, was identical to its location in control protoplasts. In addition, carbohydrate-free alkaline phosphatase was found in vacuoles from tunicamycin-treated protoplasts. Our findings indicate that the asparagine-linked carbohydrate moiety does not determine the cellular location of the enzyme.

Extent of alkaline phosphatase cytochemistry vs. extent of tetracycline fluorescence in the evaluation of histodynamic variables of bone formation

Bone ◽  
1995 ◽  
Vol 16 (5) ◽  
pp. 493-498 ◽  
Author(s):  
P. Ballanti ◽  
G. Coen ◽  
F. Taggi ◽  
S. Mazzaferro ◽  
I. Perruzza ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Bone Formation ◽  
Phosphatase Cytochemistry

scholarly journals Light microscope and electron microscope alkaline phosphatase cytochemistry of rat bone marrow leukocytes.

1979 ◽  
Vol 27 (2) ◽  
pp. 665-675 ◽  
Author(s):  
D M Williams ◽  
R Gillett ◽  
J E Linder
Keyword(s):  
Bone Marrow ◽  
Alkaline Phosphatase ◽  
Electron Microscope ◽  
Bone Marrow Cells ◽  
Cell Types ◽  
Granule Formation ◽  
Specific Granules ◽  
Phosphatase Cytochemistry ◽  
Specific Granule ◽  
Rat Bone

An enzyme cytochemical method yielding an osmiophilic reaction product, visible at both the light and electron microscope levels, has been applied to the study of alkaline phosphatase in rat bone marrow cells. The enzyme is present in both eosinophils and, in much smaller amounts, in neutrophils. In both cases it is present on the plasma membrane, and in eosinophils intracellular aggregations of reaction product are also seen. The specific granules in both cell types fail to react and the enzyme is first detectable at the promyelocyte stage. Thus the enzyme is demonstrable before specific granule formation begins in the neutrophil, indicating that they are not a significant site of alkaline phosphatase activity in the rat.

Evaluation of osteoblastic activity by morphometric comparison of alkaline phosphatase cytochemistry vs. tetracycline fluorescence

Bone ◽  
1992 ◽  
Vol 13 (5) ◽  
pp. A3-A3
Author(s):  
P. Ballanti ◽  
J.N. Bradbeer ◽  
E. Bonucci ◽  
G. Coen ◽  
S. Mazzaterro ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Osteoblastic Activity ◽  
Phosphatase Cytochemistry

Evaluation of osteoblastic activity by morphometric comparison of alkaline phosphatase cytochemistry vs. tetracycline fluorescence

Bone ◽  
1993 ◽  
Vol 14 (3) ◽  
pp. 321-326 ◽  
Author(s):  
P. Ballanti ◽  
J.N. Bradbeer ◽  
E. Bonucci ◽  
G. Coen ◽  
S. Mazzaferro ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Osteoblastic Activity ◽  
Phosphatase Cytochemistry

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

In Situ Localization of PPAR Gamma and Uncoupling Protein in Mouse Embryo Sections Using Digoxigenin-Labeled Riboprobes

1996 ◽  
Vol 54 ◽  
pp. 32-33
Author(s):  
C. Jennermann ◽  
S. A. Kliewer ◽  
D. C. Morris
Keyword(s):  
Alkaline Phosphatase ◽  
Room Temperature ◽  
Uncoupling Protein ◽  
Ppar Gamma ◽  
Nuclear Hormone Receptor ◽  
Full Length ◽  
Northern Analysis ◽  
Peroxisome Proliferator

Peroxisome proliferator-activated receptor gamma (PPARg) is a member of the nuclear hormone receptor superfamily and has been shown in vitro to regulate genes involved in lipid metabolism and adipocyte differentiation. By Northern analysis, we and other researchers have shown that expression of this receptor predominates in adipose tissue in adult mice, and appears first in whole-embryo mRNA at 13.5 days postconception. In situ hybridization was used to find out in which developing tissues PPARg is specifically expressed.Digoxigenin-labeled riboprobes were generated using the Genius™ 4 RNA Labeling Kit from Boehringer Mannheim. Full length PPAR gamma, obtained by PCR from mouse liver cDNA, was inserted into pBluescript SK and used as template for the transcription reaction. Probes of average size 200 base pairs were made by partial alkaline hydrolysis of the full length transcripts. The in situ hybridization assays were performed as described previously with some modifications. Frozen sections (10 μm thick) of day 18 mouse embryos were cut, fixed with 4% paraformaldehyde and acetylated with 0.25% acetic anhydride in 1.0M triethanolamine buffer. The sections were incubated for 2 hours at room temperature in pre-hybridization buffer, and were then hybridized with a probe concentration of 200μg per ml at 70° C, overnight in a humidified chamber. Following stringent washes in SSC buffers, the immunological detection steps were performed at room temperature. The alkaline phosphatase labeled, anti-digoxigenin antibody and detection buffers were purchased from Boehringer Mannheim. The sections were treated with a blocking buffer for one hour and incubated with antibody solution at a 1:5000 dilution for 2 hours, both at room temperature. Colored precipitate was formed by exposure to the alkaline phosphatase substrate nitrobluetetrazoliumchloride/ bromo-chloroindlylphosphate.

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