Inhibition of rat liver DNA polymerase by antiserum prepared against the wedge-presumed initiator of replication.
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Biomedical subjects
Publications and source records attributed to S Erhan.
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Results obtained from experiments dealing with mammalian, bacterial, phage and mitochondrial protein biosynthesis as well as certain enzymatically performed amino acid replacement studies on Kunitz trypsin inhibitor strongly suggest that protein ligation may be occuring in vivo. Amino acid substitution experiments prove the reversibility of endopeptidase reactions, and protein ligation is the reverse of endopeptidase reaction. These experiments are discussed in detail and the suggestion is made that ligation may also be useful in the repair of certain essential proteins which may become damaged.
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Proteins are the most underrated and under-used polymers: their impressive properties include infusibility, great mechanical strength and inherent adhesive capability due to a highly flexible backbone and many functional side chains. The notion of moisture sensitivity of proteins is not universally true. Barnacle cement (which can adhere to Teflon) and mussel and clam byssus, all of which are 99% protein, set in the presence of water and resist enzymatic as well as chemical degradation at ambient temperature. This observation suggests that proteins that are capable of tight three-dimensional cross-linking can overcome sensitivity to moisture and enzymatic attack. It should then be possible to achieve similar resistance by appropriate chemical manipulation of proteins, leading to cross-linking. We have achieved such a result with an ordinary protein, commercially available gelatin, which was chemically modified and then epoxidized. When cured such a material binds to metals and plastics. Any protein that has modifiable amino acids can be used for this purpose.
Whether proteins or nucleic acids were responsible for the emergence of life has been debated for a long time. Taking the observation that families of proteins display a remarkable invariance of their amino acid sequence around critical regions, such as active/binding sites, even though these proteins may represent considerable evolutionary diversity, as the naturally provided evidence of evoluntionary selection of working system, the idea is developed that: 1. Proteins had to have been first informational macromolecules that were necessary and sufficient to lead to the emergence of life; 2. it is impossible for a nucleic acid molecules to have formed, by chance, whose base sequence could yield a biologically active protein. A model is proposed to account for the emergence of the first successful cell according to this approach.
Base sequences of many transfer RNA (tRNA) species obtained from different sources contain homologous regions. These homologies, which are 6 to 20 nucleotides long, occur both within the same tRNA molecule and between many different tRNA molecules repeatedly. Since it is very unlikely an 80 or so nucleotide long tRNA molecule could have been formed at once, under primordial conditions, we propose that the homologous oligonucleotides found within the tRNA molecules to-day represent the earliest adapter from which tRNA molecules have evolved.
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