Purification and characterization of an inhibitor protein with cytochalasin-like acitvity from bovine adrenal medulla

TY - JOUR

T1 - Purification and characterization of an inhibitor protein with cytochalasin-like acitvity from bovine adrenal medulla

AU - Grumet, Martin

AU - Lin, Shin

N1 - Funding Information: We thank Dr. James A. Wilkins for providing the adrenal medulla extracts and John Loonsk for technical assistance. This work was supported by a research grant (GM-22289), a predoctoral traineeship (to M.G.), and a Research Career Development Award (GM-00241 to S.L.) from the National Institute of General Medical Sciences, and by a grant from the American Cancer Society (CD 73A).

PY - 1981/12/18

Y1 - 1981/12/18

N2 - A protein preparation with cytochalasin-like activity has been obtained from bovine adrenal medulla. Analysis by electrophoresis in SDS-polyacrylamide gels and chromatography in a Sephacryl S-200 column indicated that the inhibitor activity coincided with a 90 000 dalton polypeptide. The inhibitor decreased high-affinity binding of [3H]cytochalasin B to actin nuclei, apparently by competing with the drug for thesame binding site. At substoichometric levels, the inhibitor had a potent effect on actin filament elongation and on actin-dependent gelation of cell extracts in vitro. These results suggest that the inhibitor may be involved in the control of actin filament assembly and interaction in the adrenal medulla.

AB - A protein preparation with cytochalasin-like activity has been obtained from bovine adrenal medulla. Analysis by electrophoresis in SDS-polyacrylamide gels and chromatography in a Sephacryl S-200 column indicated that the inhibitor activity coincided with a 90 000 dalton polypeptide. The inhibitor decreased high-affinity binding of [3H]cytochalasin B to actin nuclei, apparently by competing with the drug for thesame binding site. At substoichometric levels, the inhibitor had a potent effect on actin filament elongation and on actin-dependent gelation of cell extracts in vitro. These results suggest that the inhibitor may be involved in the control of actin filament assembly and interaction in the adrenal medulla.

KW - (Bovine adrenal medulla)

KW - Cytochalasin B

KW - F-actin

KW - Inhibitor protein

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U2 - https://doi.org/10.1016/0304-4165(81)90118-5

DO - https://doi.org/10.1016/0304-4165(81)90118-5

M3 - Article

C2 - 7198489

SN - 0006-3002

VL - 678

SP - 381

EP - 387

JO - BBA - Biochimica et Biophysica Acta

JF - BBA - Biochimica et Biophysica Acta

IS - 3

ER -