Abstract
We have cloned full-length DDC cDNAs from a human hepatoma cDNA library [DDC; dopa decarboxylase; aromatic-L-amino acid decarboxylase, EC 4.1.1.28]. The protein encoded by hepatoma cells is the same as that encoded by adrenal chromaffin derived pheochromocytoma cells, despite reported differences in biochemical properties. We have confirmed the location of the DDC gene to chromosome 7 using a new panel of somatic cell hybrids, and we have localized the gene to band p11 on chromosome 7 by fluorescent in situ hybridization. The human gene retains 65% amino acid identity with Drosophila DDC (Accession No. X04426) and considerable structural similarity with other enzymes (F.R. Jackson, 1990, J. Mol. Evol. 31: 325-329, and references therein).
| Original language | English (US) |
|---|---|
| Pages (from-to) | 469-471 |
| Number of pages | 3 |
| Journal | Genomics |
| Volume | 13 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1992 |
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ASJC Scopus subject areas
- Genetics
Cite this
Human dopa decarboxylase : Localization to human chromosome 7p11 and characterization of hepatic cDNAs. / Scherer, Lisa J.; Mcpherson, John Douglas; Wasmuth, John J.; Marsh, J. Lawrence.
In: Genomics, Vol. 13, No. 2, 1992, p. 469-471.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Human dopa decarboxylase
T2 - Localization to human chromosome 7p11 and characterization of hepatic cDNAs
AU - Scherer, Lisa J.
AU - Mcpherson, John Douglas
AU - Wasmuth, John J.
AU - Marsh, J. Lawrence
PY - 1992
Y1 - 1992
N2 - We have cloned full-length DDC cDNAs from a human hepatoma cDNA library [DDC; dopa decarboxylase; aromatic-L-amino acid decarboxylase, EC 4.1.1.28]. The protein encoded by hepatoma cells is the same as that encoded by adrenal chromaffin derived pheochromocytoma cells, despite reported differences in biochemical properties. We have confirmed the location of the DDC gene to chromosome 7 using a new panel of somatic cell hybrids, and we have localized the gene to band p11 on chromosome 7 by fluorescent in situ hybridization. The human gene retains 65% amino acid identity with Drosophila DDC (Accession No. X04426) and considerable structural similarity with other enzymes (F.R. Jackson, 1990, J. Mol. Evol. 31: 325-329, and references therein).
AB - We have cloned full-length DDC cDNAs from a human hepatoma cDNA library [DDC; dopa decarboxylase; aromatic-L-amino acid decarboxylase, EC 4.1.1.28]. The protein encoded by hepatoma cells is the same as that encoded by adrenal chromaffin derived pheochromocytoma cells, despite reported differences in biochemical properties. We have confirmed the location of the DDC gene to chromosome 7 using a new panel of somatic cell hybrids, and we have localized the gene to band p11 on chromosome 7 by fluorescent in situ hybridization. The human gene retains 65% amino acid identity with Drosophila DDC (Accession No. X04426) and considerable structural similarity with other enzymes (F.R. Jackson, 1990, J. Mol. Evol. 31: 325-329, and references therein).
UR - http://www.scopus.com/inward/record.url?scp=0026635893&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026635893&partnerID=8YFLogxK
U2 - 10.1016/0888-7543(92)90275-W
DO - 10.1016/0888-7543(92)90275-W
M3 - Article
C2 - 1612608
AN - SCOPUS:0026635893
VL - 13
SP - 469
EP - 471
JO - Genomics
JF - Genomics
SN - 0888-7543
IS - 2
ER -