## Abstract A partial cDNA library was constructed from total poly A(+)βRNA isolated from the spleen of a rabbit (kappa allotype b5; heavy chain allotypes a3d12e15) that had been hyperimmunized with __Streptococcus pneumoniae__ (type III). In spite of the absence of either specific DNA probes for r
Construction of a human ventricular cDNA library and characterization of a beta myosin heavy chain cDNA clone
β Scribed by Mark A. Jandreski; Choong-Chin Liew
- Publisher
- Springer
- Year
- 1987
- Tongue
- English
- Weight
- 636 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0340-6717
No coin nor oath required. For personal study only.
β¦ Synopsis
We have constructed and characterized for the first time a complementary DNA (cDNA) clone, pHMC3, which codes for a cardiac myosin heavy chain mRNA from human heart. This clone contains a 1.7 kb DNA segment and specifies 543 amino acids of the carboxyl portion of the myosin heavy chain. The DNA sequence and encoded amino acid sequence were compared to the hamster alpha (pVHC1) and beta (pVHC2/pVHC3) cardiac myosin heavy chain cDNA and amino acid sequences and the rat cardiac myosin heavy chain sequences as well. The myosin heavy chain mRNAs are highly conserved and this is reflected in our cDNA clone. The pHMC3 clone is 87.9% homologous to the hamster alpha cDNA and 92.2% homologous to the hamster beta cDNA clones. The 3' untranslated region of pHMC3 is 64.1% homologous to the hamster beta clone while the hamster alpha myosin heavy chain shows only 25% homology to pHMC3 and exhibits extensive diversity. Similar results were obtained when pHMC3 was compared to the rat cardiac myosin heavy chain cDNA sequences. The comparisons showed that pHMC3 is a beta cardiac myosin heavy chain cDNA clone.
π SIMILAR VOLUMES
The complete amino acid sequence (1961 amino acids) of a vertebrate cellular myosin heavy chain-A was deduced from cDNA clones of a secretory rat mast cell line, the RBL-2H3 cell. The rat, human and chicken cellular myosin heavy chain-A exhibited high similarity in domains that allow binding of ATP
We have isolated the full-length human 56 kDa selenium binding protein (hSP56) cDNA clone, which is the human homolog of mouse 56 kDa selenium binding protein. The cDNA is 1,668 bp long and has an open reading frame encoding 472 amino acids. The calculated molecular weight is 52.25 kDa and the estim
3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL) is a homodimeric mitochondrial matrix enzyme that catalyzes the last step of ketogenesis. Using a human HL cDNA as a probe, we isolated a 1.4-kb mouse HL cDNA (HLM) from a mouse liver library and extended the sequence in the 5' direction, using RACE P