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From the Department of Microbiology, Mount Sinai School of Medicine of the City University of New York, 10 East 102 Street, New York, New York 10029
Abstract
Pooled IgG immunoglobulin heavy chains from five avian species were subjected to Edman degradation on an automated protein sequencer. Over 50% of each preparation was "unblocked" and suitable for automated sequencing. A single amino acid was present in greater than 90% of the positions studied. Analysis to position 24 or beyond showed unequivocally that these proteins belong in the VHIII subgroup.
The sequence studies allowed the derivation of a prototype avian sequence for the VHIII subgroup. When this avian prototype was compared with the mammalian prototype VHIII sequence, a high degree of sequence conservation was apparent. Such conservation, considered with the presence of phylogenetically associated residues in both the avian and mammalian proteins, strongly suggests that only limited numbers of germ line genes code for proteins of the VHIII subgroup.
Footnotes
1 Aided by grants from the National Science Foundation (GB 17046) and the United States Public Health Service (Al 09810) and a Grant-in-Aid from the New York Heart Association.
2 R.L.W. was aided by a fellowship from the New York Chapter of the Arthritis Foundation.
3 J.M.K. is an Established Investigator of the American Heart Association.
4 J.D.C. is the recipient of National Institutes of Health Career Development Award 6-K4-GM-35.
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