Jayabaskaran, C (1984) Antibodies specific for 1-methylguanosine as a probe of tRNA conformation. In: Biochemistry International, 8 (4). pp. 561-71.Full text not available from this repository.
Antibodies specific for 1-methylguanosine (m1G) were produced by immunization of rabbits with a bovine serum albumin conjugate of m1G. Antibodies specificity was determined by measuring the inhibition of binding of 3H-m1G trialcohol by various nucleosides or related derivatives. The relative affinities of the unpurified antibodies for various nucleosides showed that m1G trialcohol had an 8-fold higher affinity than m1G; further, guanosine and 2'-O-methylguanosine had at least a 500-fold lower affinity than m1G. The antibodies were purified on m1G-AH-Sepharose column and subsequently immobilized to Sepharose. Immobilized m1G antibodies quantitatively and exclusively retained m1G-containing oligonucleotides derived from ribonuclease A digests of 32P-labeled phage T4 tRNAPro. On the other hand, intact 32P-labeled T4 tRNAPro or its precursor RNA(s) did not bind to the same column. These findings indicate that at least a portion of m1G adjacent to the 3' end of the anticodon in intact T4 tRNAPro is not accessible for antibody binding.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Center for Biotechnology Information.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||24 Feb 2010 08:03|
|Last Modified:||24 Feb 2010 08:03|
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