scholarly journals Polymorphism of sarcoplasmic-reticulum adenosine triphosphatase of rabbit skeletal muscle

1981 ◽  
Vol 197 (1) ◽  
pp. 245-248 ◽  
Author(s):  
E Damiani ◽  
R Betto ◽  
S Salvatori ◽  
P Volpe ◽  
G Salviati ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Immunosorbent Assay ◽  
Adenosine Triphosphatase ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Enzyme Linked Immunosorbent Assay ◽  
Immunological Relationship ◽  
One Step ◽  
Membrane Bound

Antibody was raised in chickens against purified sarcoplasmic-reticulum Ca2+-activated ATPase (Ca2+-ATPase). The immunological relationship between the Ca2+-ATPase of fast-muscle and slow-muscle sarcoplasmic reticulum was investigated by a one-step and a two-step competitive enzyme-linked immunosorbent assay (ELISA). The results show marked antigenic differences between the membrane-bound Ca2+-ATPase of the sarcoplasmic-reticulum vesicles from fast muscle and slow muscle, beside differences in the membrane content of ATPase protein.

Assembly of the sarcoplasmic reticulum. Synthesis of calsequestrin and the Ca2++Mg2+-adenosme triphosphatase on membrane-bound polyribosomes

1978 ◽  
Vol 56 (6) ◽  
pp. 452-456 ◽  
Author(s):  
Donald C. Greenway ◽  
David H. MacLennan
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Sarcoplasmic Reticulum ◽  
Muscle Cell ◽  
Adenosine Triphosphatase ◽  
Secreted Proteins ◽  
Neonatal Rats ◽  
Muscle Cell Differentiation ◽  
Reticulocyte Lysate ◽  
Membrane Bound

Membrane-bound and free polyribosomes were isolated from skeletal muscle of neonatal rats and messages were translated in a rabbit reticulocyte lysate treated with a Ca2+-dependent nuclease to reduce endogenous messenger translation. Newly synthesized calsequestrin and adenosine triphosphatase (ATPase) were isolated by antibody precipitation, followed by separation of the precipitates in SDS-polyacrylamide gels. Radioactivity in calsequestrin and the ATPase were counted in gel slices. Calsequestrin and the ATPase were both found to be synthesized on membrane-bound polyribosomes. Since calsequestrin is a glycoprotein, localized in Golgi regions in early stages of muscle cell differentiation, it is probable that its synthesis follows the pathway for synthesis of secreted proteins except that its destination is the luminal space of a cellular organelle. The disposition of the ATPase during synthesis is, as yet, unknown.

scholarly journals A One-Step Enzyme-Linked Immunosorbent Assay for a Novel Osteoblast Differentiation-Promoting Compound, TAK-778 in Serum.

1999 ◽  
Vol 22 (12) ◽  
pp. 1266-1270 ◽  
Author(s):  
Tomofumi KUROKAWA ◽  
Tetsuo HOSHINO ◽  
Tsuneo ODA ◽  
Kazuhiro SAITO ◽  
Yasuaki OGAWA
Keyword(s):  
Immunosorbent Assay ◽  
Osteoblast Differentiation ◽  
Enzyme Linked Immunosorbent Assay ◽  
One Step

scholarly journals Wax-Assisted One-Step Enzyme-Linked Immunosorbent Assay on Lateral Flow Test Devices

2018 ◽  
Vol 34 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Masanori ISHII ◽  
Pattarachaya PREECHAKASEDKIT ◽  
Kentaro YAMADA ◽  
Orawon CHAILAPAKUL ◽  
Koji SUZUKI ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Lateral Flow ◽  
Enzyme Linked Immunosorbent Assay ◽  
Flow Test ◽  
One Step ◽  
Lateral Flow Test

scholarly journals Novel Polyclonal Antibody Raised against Tetrodotoxin Using Its Haptenic Antigen Prepared from 4,9-anhydrotetrodotoxin Reacted with 1,2-Ethaneditiol and Further Reacted with Keyhole Limpet Hemocyanin

Toxins ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 551 ◽  
Author(s):  
Sato ◽  
Takaishi ◽  
Yasumoto ◽  
Watabe
Keyword(s):  
Immunosorbent Assay ◽  
Polyclonal Antibody ◽  
Specific Antibody ◽  
Metabolic Pathways ◽  
Keyhole Limpet Hemocyanin ◽  
Enzyme Linked Immunosorbent Assay ◽  
Elisa System ◽  
One Step ◽  
Analytical Procedures ◽  
Specific Polyclonal Antibody

A novel polyclonal antibody against tetrodotoxin (TTX) was raised using its haptenic antigen, where 4,9-anhydroTTX was reacted with 1,2-ethanedithiol and this derivative was further reacted with keyhole limpet hemocyanin (KLH). This newly designed antigen (KLH-TTX) was inoculated into rabbits, resulting in the production of the specific polyclonal antibody, which reacted well with TTX and its analogs, 4-epiTTX, 11-oxoTTX and 5,6,11-trideoxyTTX, except for 4,9-anhydroTTX. The enzyme-linked immunosorbent assay (ELISA) system using this specific antibody was also developed in the present study. This newly developed polyclonal antibody with analytical procedures using direct one-step ELISA is useful to detect TTX and its analogs in toxic organisms and also disclose the mechanisms involved in their metabolic pathways and accumulation of TTX.

Development of an enzyme-linked immunosorbent assay (ELISA) for quantification of skeletal muscle calpastatin.

1996 ◽  
Vol 74 (11) ◽  
pp. 2679 ◽  
Author(s):  
M E Doumit ◽  
S M Lonergan ◽  
J R Arbona ◽  
J Killefer ◽  
M Koohmaraie
Keyword(s):  
Skeletal Muscle ◽  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay

Rapid anisotropic motion of the Ca2+-transport ATPase of the rabbit skeletal muscle sarcoplasmic reticulum

1977 ◽  
Vol 55 (6) ◽  
pp. 587-596 ◽  
Author(s):  
Barbara A. Manuck ◽  
Brian D. Sykes
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Relaxation Times ◽  
Rotational Correlation Time ◽  
Rabbit Skeletal Muscle ◽  
Nuclear Spin Relaxation ◽  
Anisotropic Model ◽  
Transport Atpase ◽  
Anisotropic Motion ◽  
Membrane Bound

1H nuclear magnetic resonance techniques were used to study the binding of uridine 5′-triphosphate to the Ca2+-transport ATPase (EC 3.6.1.3) of sarcoplasmic reticulum vesicles from rabbit skeletal muscle. The nuclear spin relaxation times determined for the bound nucleotide are used to characterize the rotational motion of the ATPase to which the nucleotide is bound. The results, assuming an anisotropic model for the motion of the ATPase in the membrane, place a low upper limit on the rotational correlation time of the ATPase. This indicates that the motion of the ATPase in the membrane is quite rapid when compared, for example, with the motion found for other membrane-bound proteins such as rhodopsin.

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