A tyrosine protein kinase activity has been detected in the mitochondrial fraction purified from human fibroblasts. By enzymatic and sedimentation analysis this activity appeared to be localized in the mitochondrial outer membrane. Mitochondrial tyrosine phosphorylation was strictly dependent on the
Human tumor cell membrane glycoprotein associated with protein kinase activity
✍ Scribed by Jutta Seehafer; B. Michael Longenecker; Andrew R. E. Shaw
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- French
- Weight
- 596 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
✦ Synopsis
A mouse MAb' 50H.19 raised against the human melanoma cell line MEL-T binds to carcinoma cell lines, carcinoma biopsy material, and certain epithelia of normal tissues. It immunoprecipitates two components from carcinoma cell lines, a major component of 22 kd which is 0glycorylated and a minor one of 24 kd which is additionally N-glycosylated. The immunocomplexed 50H. I9 antigen exhibits protein kinase activity with substrate-specificity for casein and phosvitin, but notfor histones. It phosphorylates on serine and threonine, but not tyrosine residues. Enzyme activity is cyclic AMP-independent.
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