Isolation and characterization of a cDNA clone encoding a thiol proteinase ofSarcocystis muriscyst mero` zoites (Apicomplexa)
✍ Scribed by Thomas Hansner; Bernd Freyer; Heinz Mehlhorn; Wolfgang Rüger
- Publisher
- Springer-Verlag
- Year
- 1999
- Tongue
- English
- Weight
- 424 KB
- Volume
- 85
- Category
- Article
- ISSN
- 1432-1955
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
We isolated a rice cDNA clone which encodes an open reading frame of 382 amino acids. Its deduced amino acid sequence corresponds to an ATP/ADP translocator protein. Its homology with a maize ATP/ADP translocator was 83.9~/o in nucleotide sequence, and 90.2~o of the amino acid level. Expression of t
We have isolated and sequenced a MAP (mitogen-activated protein) kinase-type cDNA from a tobacco (Nicotiana tabacum L.) cell suspension cDNA library by screening with a PCR fragment amplified from the same library with oligonucleotide primers corresponding to two sequences conserved in yeast and ani
Phytolacca anti-viral protein (PAP) was purified from Phytolacca leaves and the N-terminal was sequenced. A cDNA library was made from mRNAs isolated from Phytolacca leaves and cDNA clones for PAP were identified using oligonucleotide probes derived from the N-terminal amino acid sequence. The PAP-c
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