Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.4 (kinesin)
 5,033 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

C. elegans contains a microtubule binding protein that resembles both dynein and kinesin. This protein has a MgATPase activity and copurifies on both sucrose gradients and DEAE Sephadex columns with a polypeptide of Mr approximately 400 kd. The ATPase activity is 50% inhibited by 10 microM vanadate, 1 mM N-ethyl maleimide, or 5 mM AMP-PNP; it is enhanced 50% by 0.2% Triton. The 400 kd polypeptide is cleaved at a single site by ultraviolet light in the presence of ATP and vanadate. In these ways, the protein resembles dynein. The protein also promotes ATP-dependent translocation of microtubules or axonemes, "plus" ends trailing. This property is kinesin-like; however, the motility is blocked by 5 microM vanadate, 1 mM N-ethyl maleimide, 0.5 mM ATP-gamma-S, or by ATP-vanadate-UV cleavage of the 400 kd polypeptide, characteristics that differ from kinesin. We propose that this protein is a novel microtubule translocator.
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PMID:Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans. 295 72

A novel protein with ATPase activity was purified from the cytoplasmic extracts of maize pollen by acetone precipitation, ammonium sulfate fractionation, followed by DEAE-Sephadex A(50) and Mono S ion-exchange chromatography. The molecular weight was about 28 kD as determined by SDS-PAGE and the isoelectric point was pH 8.3 by IEF-PAGE. Western blotting analysis showed the 28 kD protein had no specific immuno-reactions with the anti-kinesin monoclonal or the anti-dynamin polyclonal antibodies. The maximum ultraviolet absorbance was at 278 nm, CD spectrum analysis showed the that 28 kD protein with the feature of a globulin. Pharmacological studies indicated that the enzyme activity was strongly inhibited by Na(3)VO(4) but insensitive to NEM. It was inhibited about 50% by NaF. Oligomycin, KNO(3) and ouabain had no effects on its ATPase activity.
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PMID:Purification of the 28 kD Protein from Maize Pollen and Studies on Its Properties. 1223 28