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Purification and properties of adenosine triphosphatase solubilized from beef heart mitochondria by chloroform

✍ Scribed by Jan Kopecký; Josef Houštěk; Zdeněk Drahota

Publisher
Springer
Year
1977
Tongue
English
Weight
289 KB
Volume
18
Category
Article
ISSN
0300-8177

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✦ Synopsis

Soluble, oligomycin-insensitive ATPase released from beef heart mitchondria by chloroform extraction can be further purified by Sepharose 6B gel filtration. This purification increases enzyme activity 4--5 times (100-130U/mg). According to specific activity, high purity and ability to reconstitute oligomycin-sensitive complex, isolated ATPase is quite comparable with enzyme preparations isolated by other methods.

📜 SIMILAR VOLUMES

Physical and enzymatic properties of nuc
Physical and enzymatic properties of nucleotide-depleted beef heart mitochondrial adenosine triphosphatase
✍ Garrett, Neil E. ;Penefsky, Harvey S. 📂 Article 📅 1975 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 535 KB

## Abstract Tightly bound adenine nucleotides are removed from multiple binding sites on beef heart mitochondrial ATPase (F~1~) by chromatography on columns of Sephadex equilibrated with 50% glycerol. Release of nucleotides from the enzyme is associated with large decreases in sedimentation velocit