Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro

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Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro. / Olesen, O. F.

In: Journal of Biological Chemistry, Vol. 269, No. 52, 1994, p. 32904-32908.

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

Harvard

Olesen, OF 1994, 'Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro', Journal of Biological Chemistry, vol. 269, no. 52, pp. 32904-32908. https://doi.org/10.1016/S0021-9258(20)30076-4

APA

Olesen, O. F. (1994). Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro. Journal of Biological Chemistry, 269(52), 32904-32908. https://doi.org/10.1016/S0021-9258(20)30076-4

Vancouver

Olesen OF. Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro. Journal of Biological Chemistry. 1994;269(52):32904-32908. https://doi.org/10.1016/S0021-9258(20)30076-4

Author

Olesen, O. F. / Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro. In: Journal of Biological Chemistry. 1994 ; Vol. 269, No. 52. pp. 32904-32908.

Bibtex

@article{da7cb0e558ea4046bef443a53bf15ef7,
title = "Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro",
abstract = "In rat brain, the microtubule-associated protein 2 (MAP2) contains two low molecular weight isoforms, consisting of 467 and 498 amino acids and designated MAP2c and d, respectively. The present study describes the expression of these isoforms in Escherichia coli and their subsequent purification to homogeneity. On SDS-polyacrylamide gel electrophoresis, the recombinant proteins ran with apparent molecular masses of 69 and 74 kDa. A microtubule-assembling assay demonstrated that the recombinant protein was biologically active and that the tubulin polymerization rate for MAP2d was twice as fast as that for MAP2c. After dephosphorylation with alkaline phosphatase, preparations of low molecular weight MAP2 from fetal rat brain aligned with recombinant MAP2c. Moreover, recombinant MAP2c could be phosphorylated with a brain extract kinase activity, resulting in a reduced electrophoretic mobility similar to that observed in fetal MAP2.",
author = "Olesen, {O. F.}",
year = "1994",
doi = "10.1016/S0021-9258(20)30076-4",
language = "English",
volume = "269",
pages = "32904--32908",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "52",

}

RIS

TY - JOUR

T1 - Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro

AU - Olesen, O. F.

PY - 1994

Y1 - 1994

N2 - In rat brain, the microtubule-associated protein 2 (MAP2) contains two low molecular weight isoforms, consisting of 467 and 498 amino acids and designated MAP2c and d, respectively. The present study describes the expression of these isoforms in Escherichia coli and their subsequent purification to homogeneity. On SDS-polyacrylamide gel electrophoresis, the recombinant proteins ran with apparent molecular masses of 69 and 74 kDa. A microtubule-assembling assay demonstrated that the recombinant protein was biologically active and that the tubulin polymerization rate for MAP2d was twice as fast as that for MAP2c. After dephosphorylation with alkaline phosphatase, preparations of low molecular weight MAP2 from fetal rat brain aligned with recombinant MAP2c. Moreover, recombinant MAP2c could be phosphorylated with a brain extract kinase activity, resulting in a reduced electrophoretic mobility similar to that observed in fetal MAP2.

AB - In rat brain, the microtubule-associated protein 2 (MAP2) contains two low molecular weight isoforms, consisting of 467 and 498 amino acids and designated MAP2c and d, respectively. The present study describes the expression of these isoforms in Escherichia coli and their subsequent purification to homogeneity. On SDS-polyacrylamide gel electrophoresis, the recombinant proteins ran with apparent molecular masses of 69 and 74 kDa. A microtubule-assembling assay demonstrated that the recombinant protein was biologically active and that the tubulin polymerization rate for MAP2d was twice as fast as that for MAP2c. After dephosphorylation with alkaline phosphatase, preparations of low molecular weight MAP2 from fetal rat brain aligned with recombinant MAP2c. Moreover, recombinant MAP2c could be phosphorylated with a brain extract kinase activity, resulting in a reduced electrophoretic mobility similar to that observed in fetal MAP2.

UR - https://www.mendeley.com/catalogue/61d812fa-9983-344e-abc9-28ba58e7f131/

U2 - 10.1016/S0021-9258(20)30076-4

DO - 10.1016/S0021-9258(20)30076-4

M3 - Journal article

C2 - 7806517

VL - 269

SP - 32904

EP - 32908

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 52

ER -

ID: 252063968