1963
DOI: 10.1093/oxfordjournals.jbchem.a127737
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Immunological Heterogeneity of Rabbit Antibody Fragments against Taka-amylase A

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1965
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Cited by 13 publications
(2 citation statements)
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“…It was found that in the presence of antibody, the rate of catalysis of L-glutamine was significantly increased over normal serum controls. This is similar to the results of Pollock (24) with penicillinase, Okada et al (22) with amylase, Rotman and Celada (25) with ,8-galactosidase, and Suzuki et al (28) with ribonuclease. A probable mechanism for this effect is that constraint placed on the enzyme by bound antibody prevents conformative changes usually imposed by normal substrate (30,31).…”
Section: Discussionsupporting
confidence: 89%
“…It was found that in the presence of antibody, the rate of catalysis of L-glutamine was significantly increased over normal serum controls. This is similar to the results of Pollock (24) with penicillinase, Okada et al (22) with amylase, Rotman and Celada (25) with ,8-galactosidase, and Suzuki et al (28) with ribonuclease. A probable mechanism for this effect is that constraint placed on the enzyme by bound antibody prevents conformative changes usually imposed by normal substrate (30,31).…”
Section: Discussionsupporting
confidence: 89%
“…Since this stimulatory activity is also present in the gamma globulin fractions of the antisera, it is likely due to the interaction of a specific antibody with the tubulin molecule, although verification of this point will rest on the purification of the specific anti-tubulin immunoglobulin from the total globulin fractions used here. While the nature of this interaction is not understood at present, it is possible that just as antibodies against various enzymes have been observed to increase the activity of the enzymes by causing conformational changes when the antibody binds to the enzyme (21)(22)(23)(24)(25), so antibody in our antisera may alter the colchicine-binding site in a similar way.…”
Section: Resultsmentioning
confidence: 99%