HELP!!!

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 (Yoshid
a
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 cutaneou
s
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, whic
h
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 e
t
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 1
4
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 tha
t
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 line
s
the AChR channel pore. The patient was previously reported by Chauplannaz an
d
Bady (1994). Functional expression studies suggested that the T254I mutation
stabilized the open state of the AChR channel
C:\Disease_Database_TongBoon_Dec2005_Mar
ch2006\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 failedGood god! Please post a description of the source data, rather than posting
a
big blob. Also see http://www.aspfaq.com/etiquette.asp?id=5006 for some
pointers.
How are you importing this? Where are you importing it to? Where is it from?
What is the structure of the source, and what of the destination?
ML
http://milambda.blogspot.com/|||What vesrion are you using?
"urgent" <urgent@.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_Mar
ch2006\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
>|||
this is my new nick i am urgen log in with another email thi post is being
transfer to another title call trouble with bcp ....2005