Rat testis mitochondrial adenylate cyclase. Partial purification and characterization

Sorel Sulimovici, Benjamin Bartoov, Bruno Lunenfeld

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


1. 1.|Adenylate cylase (EC from rat testis mitochondria has been solubilized by treatment with the non-ionic detergent Lubrol PX. The soluble enzyme was further purified by DEAE-cellulose chromatography. 2. 2.|The specific activity of the adenylate cylase eluted from the DEAE-cellulose column was found to be four times higher than that of an intact mitochondrial preparation. At this step the enzyme shows a sedimentation coefficient of 4.2 S and a diffusion coefficient (D) of 3.12·10-17 cm2/sec. 3. 3.|Solubilization of the adenylate cyclase resulted in loss of responsiveness to gonadotrophic hormones. Addition of phosphatidylserine to the soluble preparation partially restored the activation of adenylate cyclase by human chorionic gonadotrophin. 4. 4.|The results of this study suggest that the activity of the adenylate cyclase may be dependent on the membrane-bound phospholipids and that the enzyme attached to the mitochondrial membranes has some properties which are similar to the adenylate cyclase found to be associated with other membrane systems of the cell.

Original languageEnglish
Pages (from-to)454-462
Number of pages9
JournalBBA - Enzymology
Issue number2
StatePublished - 19 Feb 1975
Externally publishedYes

Bibliographical note

Funding Information:
This study was supported by Ford Foundation Grant No. 67--470. The skillful assistance of Mrs M. Kaufman and B. Druker is greatly appreciated.


Dive into the research topics of 'Rat testis mitochondrial adenylate cyclase. Partial purification and characterization'. Together they form a unique fingerprint.

Cite this