Calmodulin binding to secretory granules isolated from bovine neurohypophyses

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Calmodulin binding to secretory granules isolated from bovine neurohypophyses. / OLSEN, S. F.; SLANINOVA, J.; TREIMAN, M.; SÆRMARK, T.; THORN, N. A.

In: Acta Physiologica Scandinavica, Vol. 118, No. 4, 1983, p. 355-359.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

OLSEN, SF, SLANINOVA, J, TREIMAN, M, SÆRMARK, T & THORN, NA 1983, 'Calmodulin binding to secretory granules isolated from bovine neurohypophyses', Acta Physiologica Scandinavica, vol. 118, no. 4, pp. 355-359. https://doi.org/10.1111/j.1748-1716.1983.tb07283.x

APA

OLSEN, S. F., SLANINOVA, J., TREIMAN, M., SÆRMARK, T., & THORN, N. A. (1983). Calmodulin binding to secretory granules isolated from bovine neurohypophyses. Acta Physiologica Scandinavica, 118(4), 355-359. https://doi.org/10.1111/j.1748-1716.1983.tb07283.x

Vancouver

OLSEN SF, SLANINOVA J, TREIMAN M, SÆRMARK T, THORN NA. Calmodulin binding to secretory granules isolated from bovine neurohypophyses. Acta Physiologica Scandinavica. 1983;118(4):355-359. https://doi.org/10.1111/j.1748-1716.1983.tb07283.x

Author

OLSEN, S. F. ; SLANINOVA, J. ; TREIMAN, M. ; SÆRMARK, T. ; THORN, N. A. / Calmodulin binding to secretory granules isolated from bovine neurohypophyses. In: Acta Physiologica Scandinavica. 1983 ; Vol. 118, No. 4. pp. 355-359.

Bibtex

@article{28719b57f41544df87ef1c954727ff7f,
title = "Calmodulin binding to secretory granules isolated from bovine neurohypophyses",
abstract = "Secretory granules, isolated from bovine neurohypophyses on isoosmolar Percoll‐sucrose‐EGTA gradients had a calmodulin content of 0.09 ± 0.01 μg/mg protein (SE, n = 6). The distribution of calmodulin on the gradient showed that it did not copurify with the granules. Specific binding sites for calmodulin with a high affinity (Kd = 2.43 ± 0.27 × 10‐9 M (SE, n = 5)) and a maximum binding capacity of 1.3 ± 0.4 pmol/mg protein (SE, n = 5) could be demonstrated when such secretory granules were incubated with 125I‐calmodulin.",
keywords = "binding sites, calmodulin, calmodulin contents, granule membranes, Neurohypophysis, secretory granules",
author = "OLSEN, {S. F.} and J. SLANINOVA and M. TREIMAN and T. S{\AE}RMARK and THORN, {N. A.}",
year = "1983",
doi = "10.1111/j.1748-1716.1983.tb07283.x",
language = "English",
volume = "118",
pages = "355--359",
journal = "Acta Physiologica",
issn = "0370-839X",
publisher = "John Wiley & Sons, Ltd (10.1111)",
number = "4",

}

RIS

TY - JOUR

T1 - Calmodulin binding to secretory granules isolated from bovine neurohypophyses

AU - OLSEN, S. F.

AU - SLANINOVA, J.

AU - TREIMAN, M.

AU - SÆRMARK, T.

AU - THORN, N. A.

PY - 1983

Y1 - 1983

N2 - Secretory granules, isolated from bovine neurohypophyses on isoosmolar Percoll‐sucrose‐EGTA gradients had a calmodulin content of 0.09 ± 0.01 μg/mg protein (SE, n = 6). The distribution of calmodulin on the gradient showed that it did not copurify with the granules. Specific binding sites for calmodulin with a high affinity (Kd = 2.43 ± 0.27 × 10‐9 M (SE, n = 5)) and a maximum binding capacity of 1.3 ± 0.4 pmol/mg protein (SE, n = 5) could be demonstrated when such secretory granules were incubated with 125I‐calmodulin.

AB - Secretory granules, isolated from bovine neurohypophyses on isoosmolar Percoll‐sucrose‐EGTA gradients had a calmodulin content of 0.09 ± 0.01 μg/mg protein (SE, n = 6). The distribution of calmodulin on the gradient showed that it did not copurify with the granules. Specific binding sites for calmodulin with a high affinity (Kd = 2.43 ± 0.27 × 10‐9 M (SE, n = 5)) and a maximum binding capacity of 1.3 ± 0.4 pmol/mg protein (SE, n = 5) could be demonstrated when such secretory granules were incubated with 125I‐calmodulin.

KW - binding sites

KW - calmodulin

KW - calmodulin contents

KW - granule membranes

KW - Neurohypophysis

KW - secretory granules

U2 - 10.1111/j.1748-1716.1983.tb07283.x

DO - 10.1111/j.1748-1716.1983.tb07283.x

M3 - Journal article

C2 - 6314746

AN - SCOPUS:0020514180

VL - 118

SP - 355

EP - 359

JO - Acta Physiologica

JF - Acta Physiologica

SN - 0370-839X

IS - 4

ER -

ID: 307740287