"urgent" <urg***@discussions.microsoft.com> wrote in message
news:89CCAC1D-8F47-4D01-A35D-25254C26BD9B@microsoft.com...
> please help me create the table for the data in the following data lines
> after this
> i am out of my wits to thing for what data type to use. because for
> everything i tried i got the error below the column name will be for the
> table i appreciate a lot if someone can help me .
>
>
> column 1 column 2                                column 3
> OMIM_Name No.of av                             Description
> 100650 .0001 ALCOHOL INTOLERANCE, ACUTE ACETALDEHYDE DEHYDROGENASE 2,
> ALLELE
> 2, INCLUDED; ALDH2*2, INCLUDED ALDH2, GLU487LYS The ALDH2*2-encoded
> protein
> has a change from glutamic acid (glutamate) to lysine at residue 487
> (Yoshida
> et al., 1984). Hempel et al. (1985) and Hsu et al. (1985) also showed that
> the catalytic deficiency in mitochondrial ALDH in Orientals can be traced
> to
> a structural point mutation at amino acid position 487 of the polypeptide.
> A
> substitution of lysine for glutamic acid results from a transition of G-C
> to
> A-T. To study the mechanism by which the ALDH2*2 allele exerts its
> dominant
> effect in decreasing ALDH2 activity in liver extracts and producing
> cutaneous
> flushing when the subject drinks alcohol, Xiao et al. (1995) cloned
> ALDH2*1
> cDNA and generated the ALDH2*2 allele by site-directed mutagenesis. These
> cDNAs were transduced using retroviral vectors into HeLa and CV1 cells,
> which
> do not express ALDH2. The normal allele directed synthesis of
> immunoreactive
> ALDH2 protein with the expected isoelectric point and increased aldehyde
> dehydrogenase activity. The ALDH2*2 allele directed synthesis of mRNA and
> immunoreactive protein, but the protein lacked enzymatic activity. When
> ALDH2*1-expressing cells were transduced with ALDH2*2 vectors, both mRNAs
> were expressed and immunoreactive proteins with isoelectric points ranging
> between those of the 2 gene products were present, indicating that the
> subunits formed heteromers. ALDH2 activity in these cells was reduced
> below
> that of the parental ALDH2*1-expressing cells. Thus, the authors concluded
> that ALDH2*2 allele is sufficient to cause ALDH2 deficiency in vitro. Xiao
> et
> al. (1996) referred to the ALDH2 enzyme encoded by the ALDH2*1 allele (the
> wildtype form) as ALDH2E and the enzyme subunit encoded by ALDH2*2 as
> ALDH2K.
> They found that the ALDH2E enzyme was very stable, with a half-life of at
> least 22 hours. ALDH2K, on the other hand, had an enzyme half-life of only
> 14
> hours. In cells expressing both subunits, most of the subunits assemble as
> heterotetramers, and these enzymes had a half-life of 13 hours. Thus, the
> effect of ALDH2K on enzyme turnover is dominant. Their studies indicated
> that
> ALDH2*2 exerts its dominant effect both by interfering with the catalytic
> activity of the enzyme and by increasing its turnover. Because genetic
> epidemiologic studies have suggested a mechanism by which homozygosity for
> the ALDH2*2 allele inhibits the development of alcoholism in Asians, Peng
> et
> al. (1999) recruited 18 adult Han Chinese men, matched by age, body-mass
> index, nutritional state, and homozygosity at the ALDH2 gene loci from a
> population of 273 men. Six individuals were chosen for each of the 3 ALDH2
> allotypes, i.e., 2 homozygotes and 1 heterozygote. Following a low dose of
> ethanol, homozygous ALDH2*2 individuals were found to be strikingly
> responsive with pronounced cardiovascular hemodynamic effects as well as
> subjective perception of general discomfort for as long as 2 hours
> following
> ingestion. Among 71 Japanese nondrinkers and 268 drinkers of alcohol, Liu
> et
> al. (2005) found that drinkers had a significantly higher frequency of the
> 487glu allele. Individuals with the 487lys allele had an increased risk of
> alcohol-induced flushing (odds ratio of 33.0)
> 100690 .0001 MYASTHENIC SYNDROME, CONGENITAL, SLOW-CHANNEL CHRNA1,
> ASN217LYS
> In a 30-year-old woman with slow-channel congenital myasthenic syndrome
> (601462), Engel et al. (1996) identified a heterozygous 651C-G
> transversion
> in exon 6 of the CHRNA1 gene, resulting in an asn217-to-lys (N217K)
> substitution at a conserved residue in the M1 transmembrane domain. The
> mutation cosegregated with the disease through 3 generations. Functional
> expression studies showed that the N217K mutation slowed the rate of AChR
> channel closure, increased the apparent affinity for ACh, and enhanced
> desensitization. Cationic overload of the postsynaptic region caused an
> endplate myopathy
> 100690 .0002 MYASTHENIC SYNDROME, CONGENITAL, SLOW-CHANNEL CHRNA1,
> VAL156MET
> In a patient with SCCMS (601462), Croxen et al. (1997) identified a
> heterozygous 466G-A transition in the CHRNA1 gene, resulting in a
> val156-to-met (V156M) substitution in a putative ACh-binding region of the
> protein. Functional studies suggested that the V156M mutation stabilizes
> the
> open state of the AChR channel
> 100690 .0003 MYASTHENIC SYNDROME, CONGENITAL, SLOW-CHANNEL CHRNA1,
> THR254ILE
> In a 60-year-old woman whose myasthenic syndrome (SCCMS; 601462) had first
> become symptomatic at the age of 16, Croxen et al. (1997) identified a
> heterozygous 761C-T transition in the CHRNA1 gene, resulting in a
> thr254-to-ile (T254I) substitution in the M2 transmembrane domain which
> lines
> the AChR channel pore. The patient was previously reported by Chauplannaz
> and
> Bady (1994). Functional expression studies suggested that the T254I
> mutation
> stabilized the open state of the AChR channel
>
>
>
> C:\Disease_Database_TongBoon_Dec2005_March2006\Results>bcp OMIM.dbo.av in
> AVoutp
> ut_less_then_100.txt -c -T
>
> Starting copy...
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
> SQLState = 22001, NativeError = 0
> Error = [Microsoft][SQL Native Client]String data, right truncation
>
> BCP copy in failed
>
>