FLUORESCENT ANTIBODY STAINING IN THE SERODIAGNOSIS OF TRICHINOSIS

1963 ◽  
Vol 9 (4) ◽  
pp. 625-628 ◽  
Author(s):  
R. K. Baratawidjaja ◽  
Ann Hewson ◽  
N. A. Labzoffsky
Keyword(s):  
Complement Fixation ◽  
Trichinella Spiralis ◽  
Fluorescent Antibody ◽  
Immunofluorescent Staining ◽  
Staining Procedure ◽  
Fluorescent Staining ◽  
Antibody Staining ◽  
Human Sera ◽  
Fluorescent Antibody Staining

A fluorescent staining procedure for Trichinella spiralis and the appearance of the stained larvae are described. The applicability of the method to the sero-diagnosis of trichinosis was investigated. The results obtained both with the experimental and human sera agreed well with the complement-fixation results. In titrating 9 experimental sera and 36 sera from parasitologically proved or clinically diagnosed cases of trichinosis in humans, higher titers were obtained by the immunofluorescent staining, indicating that this test is somewhat more sensitive.

Serological relationships among flagella of Erwinia carotovora var. atroseptica and some E. carotovora var. carotovora serogroups

1980 ◽  
Vol 26 (5) ◽  
pp. 567-571 ◽  
Author(s):  
S. H. De Boer
Keyword(s):  
Cell Wall ◽  
Fluorescent Antibody ◽  
Erwinia Carotovora ◽  
Staining Procedure ◽  
Whole Cells ◽  
Bacterial Flagella ◽  
Antibody Staining ◽  
The Common ◽  
Somatic Antigens ◽  
Fluorescent Antibody Staining

The 2 Erwinia carotovora var. atroseptica serogroups and 2 out of 16 E. carotovora var. carotovora serogroups previously established on the basis of diffusible somatic antigens were shown to be serologically related by agglutination procedures using whole cells. The common agglutinating antigen in serogroups I, III, V, and XVIII was heat labile and identified as the bacterial flagella by the fluorescent antibody staining procedure. A few strains in serogroups I and III apparently lacked flagella altogether. Fluorescent antibody staining of whole cells also confirmed that the cell wall antigens of serogroups I, II, and XVIII were related and that the cell wall antigens of serogroups III and V were not related to each other or to the other serogroups.

scholarly journals Mycoplasmas in cell cultures from rheumatoid synovial membranes

1971 ◽  
Vol 69 (1) ◽  
pp. 17-25 ◽  
Author(s):  
K. B. Fraser ◽  
P. V. Shirodaria ◽  
Margaret Haire ◽  
D. Middleton
Keyword(s):  
Rheumatoid Arthritis ◽  
Tissue Culture ◽  
Fluorescent Antibody ◽  
Fluorescent Staining ◽  
Antibody Staining ◽  
Synovial Fluids ◽  
Direct Fluorescent Antibody ◽  
The Common ◽  
Synovial Membranes ◽  
Fluorescent Antibody Staining

SUMMARYTen strains of myocoplasmas were recovered from cultures of synovium or cultures inoculated with synovial fragments from rheumatoid arthritis and one from osteo-arthritis. The source of the organisms is not known. Patients with rheumatoid arthritis had no complement-fixing antibody and no fluorescent staining antibody against the mycoplasmas isolated and no mycoplasma antigen was detected by immunofluorescence in sections of synovia and in synovial fluids.The strains isolated were of two main serological types and could be distinguished by direct fluorescent antibody staining from standard types of human commensals and the common tissue-culture contaminants. One may beMycoplasma laidlawii.

Profilin is predominantly associated with monomeric actin in Acanthamoeba

1999 ◽  
Vol 112 (21) ◽  
pp. 3779-3790 ◽  
Author(s):  
D.A. Kaiser ◽  
V.K. Vinson ◽  
D.B. Murphy ◽  
T.D. Pollard
Keyword(s):  
Monoclonal Antibodies ◽  
Plasma Membrane ◽  
Fluorescent Antibody ◽  
Gel Filtration ◽  
Live Cells ◽  
A431 Cells ◽  
Antibody Staining ◽  
Large Particles ◽  
Biochemical Fractionation ◽  
Fluorescent Antibody Staining

We used biochemical fractionation, immunoassays and microscopy of live and fixed Acanthamoeba to determine how much profilin is bound to its known ligands: actin, membrane PIP(2), Arp2/3 complex and polyproline sequences. Virtually all profilin is soluble after gentle homogenization of cells. During gel filtration of extracts on Sephadex G75, approximately 60% of profilin chromatographs with monomeric actin, 40% is free and none voids with Arp2/3 complex or other large particles. Selective monoclonal antibodies confirm that most of the profilin is bound to actin: 65% in extract immunoadsorption assays and 74–89% by fluorescent antibody staining. Other than monomeric actin, no major profilin ligands are detected in crude extracts. Profilin-II labeled with rhodamine on cysteine at position 58 retains its affinity for actin, PIP(2) and poly-L-proline. When syringe-loaded into live cells, it distributes throughout the cytoplasm, is excluded from membrane-bounded organelles, and concentrates in lamellapodia and sites of endocytosis but not directly on the plasma membrane. Some profilin fluorescence appears punctate, but since no particulate profilin is detected biochemically, these spots may be soluble profilin between organelles that exclude profilin. The distribution of profilin in fixed human A431 cells is similar to that in amoebas. Our results show that the major pool of polymerizable actin monomers is complexed with profilin and spread throughout the cytoplasm.

scholarly journals Detection ofCryptosporidium molnariOocysts from Fish by Fluorescent-Antibody Staining Assays forCryptosporidiumspp. Affecting Humans

2011 ◽  
Vol 77 (5) ◽  
pp. 1878-1880 ◽  
Author(s):  
Rona Barugahare ◽  
Michelle M. Dennis ◽  
Joy A. Becker ◽  
Jan Šlapeta
Keyword(s):  
Ribosomal Dna ◽  
Fluorescent Antibody ◽  
Small Subunit ◽  
Rapid Diagnosis ◽  
Antibody Staining ◽  
Direct Fluorescent Antibody ◽  
Murray Cod ◽  
Diagnosis Of Infection ◽  
Formalin Fixed ◽  
Fluorescent Antibody Staining

ABSTRACTThree direct fluorescent-antibody staining assay kits for the detection of zoonoticCryptosporidiumspecies were used to detectCryptosporidium molnarifrom Murray cod, and the cryptosporidia were characterized by using small-subunit (SSU) ribosomal DNA (rDNA). To facilitate rapid diagnosis of infection, this study demonstrated that all three kits detected freshC. molnariand two kits detected formalin-fixed oocysts.

scholarly journals Localization of creatine kinase isoenzymes in myofibrils. II. Chicken heart muscle.

1977 ◽  
Vol 75 (2) ◽  
pp. 318-325 ◽  
Author(s):  
T Wallimann ◽  
H J Kuhn ◽  
G Pelloni ◽  
D C Turner ◽  
H M Eppenberger
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Heart Muscle ◽  
Fluorescent Antibody ◽  
Immunofluorescent Staining ◽  
Absolute Amount ◽  
Chicken Heart ◽  
Antibody Staining ◽  
Line Region ◽  
Almost All

Chicken heart muscle contains almost exclusively the BB isoenzyme of creatine kinase (CK), its myofibrils, moreover, lack an M-line. This tissue thus provides an interesting contrast to skeletal muscle, in which some of the MM-CK present as predominant CK isoenzyme is bound at the myofibrillar M-line. Approx. 2% of the total CK activity in a chicken heart homogenate remains bound to the myofibrillar fraction after repeated washing cycles; both the fraction and the absolute amount of CK bound are about threefold lower than in skeletal muscle. Almost all of the bound enzyme is located within the Z-line region of each sarcomere, as revealed by indirect fluorescent-antibody staining with antiserum against purified chicken BB-CK. After incubation with exogenous purified MM-CK, positive immunofluorescent staining for M-type CK at the H-region of heart myofibrils was observed, along with weaker fluorescence in the Z-line region. Chicken heart myofibrils may thus possess binding sites for both M and B forms of CK.

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