The complete nucleotide sequences of cDNA clones coding for human myosin light chains 1 and 3.
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Biomedical subjects
Publications and source records attributed to E Bober.
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A full-length cDNA clone coding for human mitochondrial aldehyde dehydrogenase (ALDH I) was isolated from a human fetal muscle cDNA library. Sequence analysis revealed structural similarities between the amino-terminal end of ALDH I and other known targeting sequences responsible for protein uptake into the mitochondria.
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Using monospecific antibodies against mitochondrial aldehyde dehydrogenase (ALDH I), cDNA clones were isolated from a human liver cDNA library constructed in the plasmid expression vector pEX. Two overlapping clones pEXAL21 and pEXAL43 containing inserts of 861 bp and 1180 bp respectively, code for the carboxy-terminal end of ALDH I as confirmed by sequence analysis. The messenger RNA of ALDH I was estimated by Northern blot analysis to contain approximately 2350 nucleotides. RNA hybridizations revealed that the ALDH I gene transcription is generally low in fetal tissues. Especially, transcription in the adult liver is up to 5-fold higher than in the fetal liver.
A cloned 850 bp cDNA fragment corresponding to the 3'-coding part of human ALDHI-mRNA was used as a probe for the chromosomal assignment of the ALDHI gene. Southern blot analysis of human-rodent somatic cell hybrids indicates that the human ALDHI gene resides on chromosome 12.
Human fetal muscle cDNA library was screened with a beta-myosin heavy chain gene fragment containing Alu sequences. Two cDNA clones AI and BII with 1.8 and 3 kb inserts respectively were chosen for further characterization by means of RNA and DNA hybridization procedures and sequencing. The clones appeared to contain repetitive sequences as well as single copy regions. They are actively transcribed in different stages of myogenic development but not in the liver. DNA sequence analysis of short stretches from both clones revealed no sequence homology to any other published DNA sequences.
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