Method for characterizing the nucleotide sequence of L1CAM and t

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Glycoprotein – e.g. – mucins – proteoglycans – etc.

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4353201, C07K 1400

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active

058722254

ABSTRACT:
The present invention is directed to the isolation and purification of an L1-like molecule (i.e. L1CAM) from human brain. It has been found that the isolated L1CAM molecule supports neurite growth in vitro. Applicants have also cloned and sequenced the entire coding region of human L1CAM, and found that it shows a very high degree of homology to mouse L1cam with 92% identity at the amino acid level. This similarity suggest that L1CAM is an important molecule in normal human nervous system development and nerve regeneration. Overall, there is substantially less homology to chick Ng-CAM; they are 40% identical at the amino acid level but many regions are highly conserved. Comparison of the sequences from human, mouse, chick and Drosophila, indicates that the L1 immunoglobulin domain 2 and fibronectin type III domain 2 are strongly conserved and thus are likely functionally important.

REFERENCES:
Harper et al. 1991, Journal of Neurochemistry 56(3): 797-804.
Moos et al. 1988. Nature 334:701-703.
Watson et al. Recombinant DNA; A Short Course pp. 76-78, Scientific American Books, New York.
Wallace et al. 1987. Methods in Enzymology 152:432-442.

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