scholarly journals Enzymic Formation of norAdrenaline in Mammalian Tissue Extracts

Nature ◽  
1950 ◽  
Vol 165 (4206) ◽  
pp. 926-926 ◽  
Author(s):  
KARL H. BEYER ◽  
H. BLASCHKO ◽  
J. H. BURN ◽  
H. LANGEMANN
Keyword(s):  
Mammalian Tissue ◽  
Tissue Extracts

THE DEGRADATION OF CHOLESTEROL BY MAMMALIAN TISSUE EXTRACTS

1954 ◽  
Vol 76 (15) ◽  
pp. 4048-4048 ◽  
Author(s):  
William S. Lynn ◽  
Ezra Staple ◽  
Samuel Gurin
Keyword(s):  
Mammalian Tissue ◽  
Tissue Extracts

scholarly journals ON THE PRESENCE IN SYPHILITIC SERUM OF ANTIBODIES TO SPIROCHETES, THEIR RELATION TO SO CALLED WASSERMANN REAGIN, AND THEIR SIGNIFICANCE FOR THE SERODIAGNOSIS OF SYPHILIS

1940 ◽  
Vol 71 (2) ◽  
pp. 215-230 ◽  
Author(s):  
Harry Eagle ◽  
Ralph B. Hogan
Keyword(s):  
Complement Fixation ◽  
High Titre ◽  
Beef Heart ◽  
Mammalian Tissue ◽  
Practical Utility ◽  
Tissue Extracts ◽  
Human Sera ◽  
Antigenic Material ◽  
Normal Human ◽  
Serodiagnosis Of Syphilis

1. In confirmation of Gaehtgens, syphilitic human sera give positive complement fixation with cultures of so called T. pallidum (Reiter strain). Syphilitic rabbit sera are equally reactive. Syphilitic human and rabbit sera agglutinate these cultures, often in high titre (Beck). 2. Normal rabbit sera react weakly with the culture to give both agglutination and complement fixation in low titre. Normal human sera, despite the fact that they contain agglutinins in low titre, fail to fix complement with the Reiter strain of cultured spirochetes. Confirming Gaehtgens, the latter reaction is therefore of practical utility for the serum diagnosis of syphilis. 3. When syphilitic serum is heated at 63°C., there is no demonstrable difference in the thermolability of the antibody to spirochetes, and of the reagin which determines the Wassermann and flocculation tests. 4. (a) The absorption of syphilitic serum by spirochetal suspensions removes all reactivity, not only for the spirochetes, but for tissue lipoids (alcoholic beef heart extract) as well; the sera become Wassermann- and flocculation-negative. (b) Absorption of syphilitic serum with tissue lipoids renders the Wassermann and flocculation tests negative, but does not demonstrably change the reactivity of the serum with spirochetes. (c) Rabbits immunized to beef heart lipoid develop spirochetal agglutinins and complement-fixing antibodies (Reiter strain) in high titre. 5. It is concluded that these cultured spirochetes contain antigenic material serologically related to a substance present in mammalian tissue, as well as other antigenic factors not present in such extracts, but equally reactive with syphilitic serum. 6. These findings support the thesis that the primary serologic change in syphilis is the development of antibodies to T. pallidum. The Wassermann and flocculation tests would be explained on the basis that the tissue extracts used as "antigen" in these tests contain one or more substances serologically related to antigenic components of T. pallidum. Similarly, the cultured Reiter strain of spirochete is apparently sufficiently close serologically to T. pallidum to be agglutinated by and to give complement fixation with the antibodies to T. pallidum present in syphilitic serum. 7. Since suspensions of cultured spirochetes contain antigenic factors which react specifically with syphilitic serum, some of which are not present in ordinary Wassermann and flocculation "antigens," they may prove even more valuable than those tissue extracts in the serodiagnosis of syphilis.

scholarly journals Non-enzymic nature of the pyridine haemochrome-cleaving activity of mammalian tissue extracts (‘haem α-methyl oxygenase’)

1970 ◽  
Vol 119 (5) ◽  
pp. 905-911 ◽  
Author(s):  
Emer Colleran ◽  
P. Ó Carra
Keyword(s):  
Reduced Glutathione ◽  
Reduced Form ◽  
Mammalian Tissue ◽  
Tissue Extracts ◽  
Mammalian Liver

1. The pyridine haemochrome-cleaving activity of extracts from mammalian liver and other tissues is shown conclusively to be entirely non-enzymic in nature and attributable to coupled oxidation with ascorbate. 2. Reduced glutathione probably contributes to the activity indirectly by continuously regenerating the ascorbate to the reduced form. 3. The cleavage shows no specificity for the α-methine bridge of pyridine haemochrome. 4. Results are presented suggesting some probable reasons for the erroneous characterization of the activity as an α-methine-specific haem-cleaving enzyme (`haem α-methenyl oxygenase') by Nakajima and co-workers (e.g. Nakajima, Takemura, Nakajima & Yamaoka, 1963; Nakajima & Gray, 1967).

Synthesis of sedoheptulose from non-dialyzable, endogenous substrates in mammalian tissue extracts

1981 ◽  
Vol 96 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Paul P. Hipps ◽  
Karen Ackermann ◽  
William H. Holland ◽  
William R. Sherman
Keyword(s):  
Mammalian Tissue ◽  
Tissue Extracts ◽  
Endogenous Substrates

Sulfhydryl bond formation is a prerequisite for proper cycling of centrosomes and chromosomes in mammalian tissue culture cells

1993 ◽  
Vol 51 ◽  
pp. 342-343
Author(s):  
Heide Schatten ◽  
Neidhard Paweletz ◽  
Ron Balczon
Keyword(s):  
Tissue Culture ◽  
Cell Cycle Progression ◽  
Group Formation ◽  
Sulfhydryl Group ◽  
Mammalian Tissue ◽  
Mitotic Chromosomes ◽  
Microtubule Network ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Transmission Electron

To study the role of sulfhydryl group formation during cell cycle progression, mammalian tissue culture cells (PTK2) were exposed to 100¼M 2-mercaptoethanol for 2 to 6 h during their exponential phase of growth. The effects of 2-mercaptoethanol on centrosomes, chromosomes, microtubules, membranes and intermediate filaments were analyzed by transmission electron microscopy (TEM) and by immunofluorescence microscopy (IFM) methods using a human autoimmune antibody directed against centrosomes (SPJ), and a mouse monoclonal antibody directed against tubulin (E7). Chromosomes were affected most by this treatment: premature chromosome condensation was detected in interphase nuclei, and the structure in mitotic chromosomes was altered compared to control cells. This would support previous findings in dividing sea urchin cells in which chromosomes are arrested at metaphase while the centrosome splitting cycle continues. It might also support findings that certairt-sulfhydryl-blocking agents block cyclin destruction. The organization of the microtubule network was scattered probably due to a looser organization of centrosomal material at the interphase centers and at the mitotic poles.

Fibrinolytic Activity of Lung and Spleen Extracts Observed in Conventional but not in Germ-Free Rats

1979 ◽  
Vol 42 (02) ◽  
pp. 726-733 ◽  
Author(s):  
Utako Okamoto ◽  
Jun-ichiro Yamamoto ◽  
Yoko Nagamatsu ◽  
Noboru Horie
Keyword(s):  
Serine Protease ◽  
Plasminogen Activator ◽  
Fibrinolytic Activity ◽  
Iodoacetic Acid ◽  
Thrombin Inhibitor ◽  
Rat Tissues ◽  
Germ Free ◽  
Neutral Ph ◽  
Tissue Extracts

SummaryProtease-like activity which split plasminogen-free fibrin was demonstrated in 2 M KSCN extracts of the lung and spleen of conventional rats. The activity was virtually undetectable in tissue extracts from germ-free rats. The extracts from the conventional rat tissues split fibrin and fibrinogen remarkably at neutral pH, but not casein, when examined using fibrin, fibrinogen-agar and casein-agar plates. The fibrinolytic activity was inhibited by STI and DFP, indicating a serine protease nature. The activity was not inhibited by TLCK, t-AMCHA or dansyl-L-arginine-methylpiperidine amide (a selective synthetic thrombin inhibitor, OM189). It was neither activated nor inhibited by cysteine, KCN or iodoacetic acid. The results obtained indicate that the protease-like activity of the lung and spleen extracted with 2 M KSCN from conventional rats has properties which differ from those of trypsin, plasmin, plasminogen-activator, thrombin, and cathepsin A, B and C.

In Vitro Immunodetection of Prothymosin Alpha in Normal and Pathological Conditions

2020 ◽  
Vol 27 (29) ◽  
pp. 4840-4854 ◽  
Author(s):  
Chrysoula-Evangelia Karachaliou ◽  
Hubert Kalbacher ◽  
Wolfgang Voelter ◽  
Ourania E. Tsitsilonis ◽  
Evangelia Livaniou
Keyword(s):  
Mammalian Cells ◽  
Therapeutic Potential ◽  
Prothymosin Alpha ◽  
Disease States ◽  
Leading Role ◽  
Tissue Extracts ◽  
Biologic Response ◽  
Health And Disease ◽  
Almost All

Prothymosin alpha (ProTα) is a highly acidic polypeptide, ubiquitously expressed in almost all mammalian cells and tissues and consisting of 109 amino acids in humans. ProTα is known to act both, intracellularly, as an anti-apoptotic and proliferation mediator, and extracellularly, as a biologic response modifier mediating immune responses similar to molecules termed as “alarmins”. Antibodies and immunochemical techniques for ProTα have played a leading role in the investigation of the biological role of ProTα, several aspects of which still remain unknown and contributed to unraveling the diagnostic and therapeutic potential of the polypeptide. This review deals with the so far reported antibodies along with the related immunodetection methodology for ProTα (immunoassays as well as immunohistochemical, immunocytological, immunoblotting, and immunoprecipitation techniques) and its application to biological samples of interest (tissue extracts and sections, cells, cell lysates and cell culture supernatants, body fluids), in health and disease states. In this context, literature information is critically discussed, and some concluding remarks are presented.

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