Quantification of biofilm exopolysaccharides using an in situ assay with periodic acid–Schiff reagent

2016 ◽  
Vol 500 ◽  
pp. 12-14 ◽  
Author(s):  
I. Randrianjatovo-Gbalou ◽  
E. Girbal-Neuhauser ◽  
C.-E. Marcato-Romain
Keyword(s):  
Periodic Acid ◽  
Periodic Acid Schiff ◽  
Schiff Reagent ◽  
In Situ Assay

A Study of Nuclei and Intercellular Ground Substance during the in situ Differentiation of Somites in Taricha torosa

Development ◽  
1961 ◽  
Vol 9 (4) ◽  
pp. 650-660
Author(s):  
Cyril V. Finnegan
Keyword(s):  
Morphological Changes ◽  
Periodic Acid ◽  
Ground Substance ◽  
Tail Bud ◽  
Interphase Nuclei ◽  
Taricha Torosa ◽  
Intercellular Matrix ◽  
Schiff Reagent

In order better to evaluate results obtained in this laboratory concerning the responses of differentiating postneurula somite tissue to other mesoderm tissue placed in its immediate vicinity (Finnegan, unpublished), it was necessary to examine somite differentiation in situ. A qualitative examination of somite interphase nuclei of tail-bud and later stages was performed to note their morphological changes since it was assumed, as suggested by Briggs & King (1955), that such changes indicate cellular differentiation and, conversely, that absence of such changes indicates that the cells are not actively differentiating. Because of the possible role of the intercellular matrix in histogenesis (see Grobstein, 1954, 1959; and Edds, 1958) a study was made of the development in the somite of that portion of the intercellular matrix which is demonstrable histochemically with the periodic acid-Schirf (PAS) technique. The visual clarity of the results has been materially aided by the fluorescent Schiff reagent of Culling & Vassar (1961) which makes possible a fluorescent Feulgen and a fluorescent PAS reaction.

scholarly journals The Structural Characteristics of Chicken Fibrinogen

1977 ◽  
Author(s):  
J. Pindyck ◽  
M. W. Mosesson ◽  
D. Bannerjee ◽  
D. Galanakis
Keyword(s):  
Gel Electrophoresis ◽  
Structural Characteristics ◽  
Periodic Acid ◽  
Factor Xiiia ◽  
Periodic Acid Schiff ◽  
Polymer Formation ◽  
Sensitive Site ◽  
Schiff Reagent ◽  
The One ◽  
Fibrinogen Molecule

The structure and subunit composition of chicken fibrinogen(ϕ) have been investigated. Dodecyl sulfate gel electrophoresis of unreduced specimens revealed a single ϕ band with a molecular weight of approximately 320,000. ϕ and fibrin specimens were also electrophoresed after reduction with dithiothreitol, and after crosslinking of unreduced specimens in the presence of Factor Xllla. Chromatographically separated S-sulfo chains were also studied after reptilase or thrombin treatment,and certain samples were stained with periodic acid Schiff reagent(PAS). Chicken Aα chains weresmaller than human Aα chains (54,500 vs.70,900, respectively) but, like mammalian Aα chains, they possessed a reptilase and thrombin sensitive site, were PAS negative,and undergo Factor XIIIa catalyzed α-polymer formation. The sizes of chicken Bβ and γ chains were nearly thesame as their mammalian counterparts, (i. e. 60,000 and 49,000 respectively) ; both types of chains were PAS positive. Chicken Bβ chains possessed a slowly reactive thrombin sensitive site apparently corresponding to the one in human ϕ; the chicken β chains, like mammalian β chains, did not undergo Factor XIIIa catalyzed cross-linking. Like mammalian γ chains, chicken γ chains could undergo Factor XIIIa catalyzed γ-γ dimerization and did not possess thrombin or reptilase sensitive sites. These findings indicate that the chicken fibrinogen molecule is composed of three pairs of disulfide-bridged chains corresponding in most respects to mammalian fibrinogen chains.

scholarly journals IMMUNOLOGIC STUDIES OF HEART TISSUE

1961 ◽  
Vol 113 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Melvin H. Kaplan ◽  
Frederick D. Dallenbach
Keyword(s):  
Heart Disease ◽  
Connective Tissue ◽  
Gamma Globulin ◽  
Fluorescent Antibody ◽  
Periodic Acid ◽  
Heart Tissue ◽  
Periodic Acid Schiff ◽  
Schiff Reagent ◽  
Points Of View ◽  
Rheumatic Heart

Using fluorescent antibody methods, deposits of bound gamma globulin, as determined in unfixed washed sections of auricular appendages from rheumatic hearts, were noted in a significant number (18 per cent) of 100 specimens studied. Such deposits were observed in myofibers, sarcolemma, interstitial connective tissue, and vessel walls. Albumin and fibrin were generally found absent from these sites. Control hearts from normal and pathologic material, including postmortem and biopsied specimens, in general, did not reveal such deposits. These various tissue sites which contained bound gamma globulin frequently exhibited evidence of alteration as indicated both by enhanced affinity for eosin and by strongly positive reaction with the periodic acid-Schiff reagent, and appeared comparable in some cases to "fibrinoid." Bound gamma globulin was not observed in cellular or stromal components of Aschoff lesions, nor was the occurrence of Aschoff lesions correlated with presence of bound gamma globulin. It is suggested that deposition of gamma globulin and the eosinophilic alteration associated with such deposition are related to certain of the pathologic changes of rheumatic heart disease. The nature of such deposits of gamma globulin was considered from immune and non-immune points of view.

The Properties of Soluble Proteins Synthesized by Nephrotic Rat Kidney Microsomes

1972 ◽  
Vol 50 (3) ◽  
pp. 292-298
Author(s):  
V. N. Katiyar ◽  
B. L. Dinh
Keyword(s):  
Gel Electrophoresis ◽  
Rat Kidney ◽  
Periodic Acid ◽  
Rabbit Antiserum ◽  
Periodic Acid Schiff ◽  
Rat Serum ◽  
Tissue Protein ◽  
Schiff Reagent ◽  
Normal Rat ◽  
Kidney Microsomes

The incorporation of 14C-leucine into the microsomal proteins of nephrotic rat kidney was much higher than that in the microsomal proteins of the normal rat kidney. When the newly synthesized microsomal proteins were analyzed by acrylamide gel electrophoresis, it was found that the higher incorporation of 14C-leucine in nephrotic rat kidney was mostly due to an increase in the biosynthesis of a tissue protein which migrated in the electrophoretic zone between serum albumin and transferrin. This protein did not react with rabbit antiserum to normal rat serum and was stained with periodic acid – Schiff reagent. It was believed to be excreted in the urine of nephrotic rats in great quantity and was easily identified as a distinct band in electrophoregrams of urine from these rats.

Isolation and partial characterization of a soluble mucin in human pancreatic juice

1991 ◽  
Vol 69 (8) ◽  
pp. 566-571
Author(s):  
S. P. Lee ◽  
Y. S. Choong ◽  
H. Z. Park
Keyword(s):  
Molecular Weight ◽  
Pancreatic Juice ◽  
Periodic Acid ◽  
Average Molecular Weight ◽  
Small Molecular Weight ◽  
Periodic Acid Schiff ◽  
Cellulose Acetate Electrophoresis ◽  
Cscl Density Gradient ◽  
Oligosaccharide Moiety ◽  
Schiff Reagent

Morphological and histochemical abnormalities in pancreatic mucin occur in many pancreatic disorders. However, the composition of pancreatic mucin is poorly understood. Purified mucin was isolated from pure pancreatic juice by sequential chromatography on Sepharose CL-2B and CL-4B followed by CsCl density gradient ultracentrifugation. The mucin preparation consists of 24% protein and 73% carbohydrate. Reduction of the macromolecule (> 2 × 106) by mercaptoethanol resulted in the formation of subunits of molecular weight 500 000 and released several small molecular weight proteins, including a glycoprotein of an average molecular weight of 116 000. Cellulose acetate electrophoresis separated the mucin into three species of different staining properties for periodic acid-Schiff reagent and Alcian blue, suggesting the presence of microheterogeneity with respect to sulphation and sialation. Threonine, serine, and proline composed 48% of the total amino acids, while the oligosaccharide moiety contained N-acetylglucosamine, N-acetyl-galactosamine, fucose, galactose, sialic acid, and sulphate. We also detected the presence of C16:0 and C18:0 fatty acids which were probably noncovalently bound to the pancreatic mucin.Key words: pancreas, mucin, glycoprotein, cystic fibrosis.

Human intestinal goblet cell mucin

1976 ◽  
Vol 54 (8) ◽  
pp. 707-716 ◽  
Author(s):  
I. Jabbal ◽  
D. I. C. Kells ◽  
G. Forstner ◽  
J. Forstner
Keyword(s):  
Goblet Cell ◽  
High Speed ◽  
Proteolytic Enzymes ◽  
Periodic Acid ◽  
Periodic Acid Schiff ◽  
Strong Concentration ◽  
Acid Ratio ◽  
Schiff Reagent ◽  
Major Chemical ◽  
Sepharose 4B

Goblet cell mucin (GCM) has been purified for the first time from mucosal scrapings of human small intestine. Proteolytic enzymes and organic solvents were avoided during the isolation procedure. The mucin was purified by Sepharose 4B and 2B column chromatography of high-speed supernatant fractions. The most purified fraction was compared with rat intestinal GCM. The two were similar with respect to chemical composition, antigenic features, and polyacrylamide disc gel electrophoresis. The major chemical differences included a higher hexosamine–fucose and hexosamine – sialic acid ratio in human mucin. The two mucins showed strong concentration dependence in sedimentation velocity studies. Human mucin at a concentration of 0.2 to 1.5 mg protein per millilitre gave multiple associated peaks with variable s0 values (10.8–36.6). Rat mucin, in contrast, gave a constant (although polydisperse) pattern with s0 = 15.15. To explore these differences both mucins were stained with periodic acid – Schiff reagent and subjected to band ultracentrifugation at concentrations of 0.6–1.9 μg protein per millilitre. At this low concentration, rat mucin did not change in its sedimentation characteristics. In contrast, human GCM produced a single peak with s0 = 37.9. Thus dilution abolished polydispersity in the human but not the rat mucin, suggesting that intermolecular bonding forces in the human mucin are weaker.

scholarly journals Identification of Brachyspira spp. in the cecum of broiler chickens using histology and in situ diagnostic assays

2021 ◽  
Vol 42 (5) ◽  
pp. 2813-2824
Author(s):  
Monica Regina de Matos ◽  
◽  
Aline Patrícia Grzegozevski ◽  
Alessandra da Cruz ◽  
Arthur Colombari Cheng ◽  
...  
Keyword(s):  
Broiler Chickens ◽  
Periodic Acid ◽  
Goblet Cells ◽  
Ffpe Tissue ◽  
Economic Losses ◽  
Periodic Acid Schiff ◽  
Tissue Samples ◽  
Rabbit Polyclonal Antibody ◽  
Formalin Fixed Paraffin Embedded

The genus Brachyspira corresponds to the group of bacteria formerly classified into the genus Serpulina and includes several commensal and pathogenic intestinal spirochetes that affect pigs, poultry, and other animal species, including humans. In birds, some pathogenic species of this genus causes a condition known as avian intestinal spirochetosis, which remains underdiagnosed, thereby causing serious economic losses. Brachyspira is a fastidious organism that necessitates the employment of fast and efficient identification techniques. The aim of this study was to identify Brachyspira spp. using histology, immunohistochemistry (IHC) and fluorescence in situ hybridization (FISH) in formalin-fixed paraffin embedded (FFPE) tissue samples from the cecum of commercial poultry. Samples were collected from 129 birds aged between 35 and 45 days from commercial broiler farms. For evaluation, routine histology processing (H&E) and the histochemical technique, periodic acid–Schiff (PAS) were done. Additionally, FFPE tissue samples were evaluated for FISH and IHC. The histological lesions were analyzed and graded after H&E staining, and the goblet cells were counted and compared using PAS staining with the positive and negative samples obtained through FISH and IHC. For FISH, probes labeled with Brachyspira spp., B. pilosicoli, B. hyodysenteriae, and B. intermedia were used, whereas rabbit polyclonal antibody specific for Brachyspira spp. was used for IHC. Of 129 samples, 82 were positive with IHC and 86 were positive with FISH. The samples positive for the genus Brachyspira in the FISH technique were tested for B. pilosicoli, B. hyodysenteriae, and B. intermedia in which 56 were positive for B. pilosicoli, 75 for B. hyodysenteriae and 80 for B. intermedia. There was an increase in goblet cells in the samples positive for FISH and IHC. The techniques used were effective and gave corresponding results, thus serving as a fast and efficient tool for diagnosis.

scholarly journals COMPARISON OF IMMUNOHISTOCHEMICAL MARKER WITH SPECIAL STAINS IN THE PROGNOSIS OF THE DIFFERENT GRADES OF ORAL SQUAMOUS CELL CARCINOMA

2019 ◽  
Vol 8 (4) ◽  
Author(s):  
Dr. Parthiban Nallaiyan ◽  
Dr. Bharathi Ramakrishnan ◽  
Dr. Gnanadeepam Santigo ◽  
Dr. Dhanalakshmi Jeyasivanesan
Keyword(s):  
Squamous Cell Carcinoma ◽  
Oral Squamous Cell Carcinoma ◽  
Cell Carcinoma ◽  
Squamous Cell ◽  
Periodic Acid ◽  
Collagen Fibre ◽  
Ki 67 ◽  
Periodic Acid Schiff ◽  
Schiff Reagent ◽  
Neutral Mucin

Objectives: The aim of the study is to compare the efficiency of Ki-67 with special stains in the stroma of different grades of Oral Squamous Cell Carcinoma (OSCC) and to evaluate the influence of these changes in predicting the prognosis of these tumors. Materials and Methods: A total of 30 cases of different grades of Oral Squamous Cell Carcinoma and 6 cases of control were sections and stained with Picrosirus red (PR), combined Alcian blue-periodic acid Schiff reagent (AB-PAS) and Immunohistochemical (IHC) marker Ki-67. Results: Collagen fibre nature using PR stain and proliferative activity of malignant epithelial cells using IHC marker Ki-67 was found to be statistically significant. Mucin presence using AB-PAS was statistically insignificant. Conclusion: Prognosis in different grades of oral squamous cell carcinoma can be accessed by change in collagen fibres birefringence, as the tumour progresses there is change from mature to immature collagen. Ki-67 is a good proliferative marker and shows that there is positive correlation with histological grading of oral squamous cell carcinoma. Presence of acidic or neutral mucin in OSCC needed to be further studied. For assessing the prognosis in different grades of OSCC, special stains can also be used. Keywords: Collagen, Mucin, Squamous cell carcinoma, Ki-67.

Sign in / Sign up

Export Citation Format

Share Document