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SV Reddy, ZQ Zhou, KJ Rao, JP Scott, H Watzke, KA High and P Jagadeeswaran
Department of Cellular and Structural Biology, University of Texas Health
Science Center, San Antonio.
Enzymatic amplification technique was used to isolate all eight exons and
sequences around the splice junctions, putative promoter, and
polyadenylation sites of human factor X DNA from a patient with factor X
deficiency. Two genetic changes in factor X have been observed in this
patient. The patient is most likely a compound heterozygote since there is
only 14% activity associated with factor X. A point mutation that resulted
in the substitution of cysteine (TGC) for arginine (CGC) at amino acid 366
was found in exon VIII of one allele of the factor X gene. This mutation,
which occurs in the catalytic domain, can affect the formation of a
disulfide bridge and thus could result in a reduction in factor X activity.
Sequencing all the regions revealed a second mutation: a deletion of one
nucleotide (TCCT to TCT) in exon VII that would cause a frame shift at
amino acid 272 followed by termination. We have also shown that the point
mutation in exon VIII creates an ApaL1 restriction site and destroys the
HinP1 site. Enzymatic DNA amplification followed by restriction digestion
provides a quick, reliable, and sensitive method for carrier detection and
antenatal diagnosis in affected kindreds. This is the first
characterization of factor X deficiency at the molecular level. We propose
to name this mutation Factor XSan Antonio.
This article has been cited by other articles:
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| Copyright © 1989 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
