Rapid determination of glycoproteins and glycopeptides by periodic acid Schiff reagent dot-blotting assay on nitrocellulose membrane

1993 ◽  
Vol 41 (6) ◽  
pp. 896-898 ◽  
Author(s):  
Lianglu. Wan ◽  
Robert B. van Huystee
Keyword(s):  
Rapid Determination ◽  
Periodic Acid ◽  
Nitrocellulose Membrane ◽  
Periodic Acid Schiff ◽  
Schiff Reagent ◽  
Dot Blotting

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.

scholarly journals Determination of the glycogen content in single neutrophil leukocytes using a micromodel of leukocyte glycogen.

1975 ◽  
Vol 23 (1) ◽  
pp. 59-64 ◽  
Author(s):  
G Gahrton ◽  
I Olsson ◽  
A Dahlqvist
Keyword(s):  
Periodic Acid ◽  
Liver Glycogen ◽  
Mean Value ◽  
Acid Oxidation ◽  
Periodic Acid Schiff ◽  
Periodic Acid Oxidation ◽  
Normal Human ◽  
Schiff Reaction ◽  
Neutrophil Leukocytes

The kinetics of the periodic acid oxidation as part of the periodic acid-Schiff reaction was studied by combined microinterferometry and microspectrophotometry in micromodel systems of liver glycogen and leukocyte glycogen as well as in neutrophil leukocytes. The initial formation of Schiff-positive chromogens was more rapid in neutrophil leukocytes than in liver or leukocyte glycogen. The chromogen formation was, however, practically complete within 60 min in both neutrophil leukocytes and leukocyte glycogen, but this did not appear to be the case in liver glycogen. Differences in the rate of chromogen formation may depend on various factors such as differences in the source and treatment of the glycogen. The complete periodic acid-Schiff reaction appears to be a measure of the glycogen amount in neutrophil leukocytes and the microdroplet system of leukocyte glycogen is considered to be an appropriate model for the estimation of the glycogen amount in single neutrophil leukocytes. A mean value of 13.3 10-12 g glycogen per normal human neutrophil was found.

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 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.

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