DNA polymerase α-DNA primase from human placenta Immunoaffinity purification and preliminary characterization

V. N. Podust; O. I. Lavrik; H. P. Nasheuer; F. Grosse

doi:10.1016/0014-5793(89)80181-4

DNA polymerase α-DNA primase from human placenta Immunoaffinity purification and preliminary characterization

V. N. Podust
, O. I. Lavrik
, H. P. Nasheuer
, F. Grosse

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

14 Citations (Scopus)

Abstract

Highly purified DNA polymerase α-DNA primase from normal human tissue (human placenta) has been prepared by immunoaffinity purification on immobilized anti-human DNA polymerase α monoclonal antibody SJK 287-38. According to data from SDS electrophoresis this preparation consists of subunits of 180, 160, 145, 140 kDa (a cluster of DNA-polymerizing subunits), 73 kDa (function unknown) and 59, 52 kDa (corresponding to primase). Three active enzyme forms of 270, 460 and 575 kDa have been revealed using native electrophoresis followed by detection of DNA polymerase activity.

Original language	English
Pages (from-to)	14-16
Number of pages	3
Journal	FEBS Letters
Volume	245
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(89)80181-4
Publication status	Published - 13 Mar 1989
Externally published	Yes

Keywords

(Human placenta)
DNA polymerase α
Immunoaffinity purification

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10.1016/0014-5793(89)80181-4

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abstract = "Highly purified DNA polymerase α-DNA primase from normal human tissue (human placenta) has been prepared by immunoaffinity purification on immobilized anti-human DNA polymerase α monoclonal antibody SJK 287-38. According to data from SDS electrophoresis this preparation consists of subunits of 180, 160, 145, 140 kDa (a cluster of DNA-polymerizing subunits), 73 kDa (function unknown) and 59, 52 kDa (corresponding to primase). Three active enzyme forms of 270, 460 and 575 kDa have been revealed using native electrophoresis followed by detection of DNA polymerase activity.",

keywords = "(Human placenta), DNA polymerase α, Immunoaffinity purification",

author = "Podust, \{V. N.\} and Lavrik, \{O. I.\} and Nasheuer, \{H. P.\} and F. Grosse",

year = "1989",

month = mar,

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doi = "10.1016/0014-5793(89)80181-4",

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T1 - DNA polymerase α-DNA primase from human placenta Immunoaffinity purification and preliminary characterization

AU - Podust, V. N.

AU - Lavrik, O. I.

AU - Nasheuer, H. P.

AU - Grosse, F.

PY - 1989/3/13

Y1 - 1989/3/13

N2 - Highly purified DNA polymerase α-DNA primase from normal human tissue (human placenta) has been prepared by immunoaffinity purification on immobilized anti-human DNA polymerase α monoclonal antibody SJK 287-38. According to data from SDS electrophoresis this preparation consists of subunits of 180, 160, 145, 140 kDa (a cluster of DNA-polymerizing subunits), 73 kDa (function unknown) and 59, 52 kDa (corresponding to primase). Three active enzyme forms of 270, 460 and 575 kDa have been revealed using native electrophoresis followed by detection of DNA polymerase activity.

AB - Highly purified DNA polymerase α-DNA primase from normal human tissue (human placenta) has been prepared by immunoaffinity purification on immobilized anti-human DNA polymerase α monoclonal antibody SJK 287-38. According to data from SDS electrophoresis this preparation consists of subunits of 180, 160, 145, 140 kDa (a cluster of DNA-polymerizing subunits), 73 kDa (function unknown) and 59, 52 kDa (corresponding to primase). Three active enzyme forms of 270, 460 and 575 kDa have been revealed using native electrophoresis followed by detection of DNA polymerase activity.

KW - (Human placenta)

KW - DNA polymerase α

KW - Immunoaffinity purification

UR - https://www.scopus.com/pages/publications/0024535395

U2 - 10.1016/0014-5793(89)80181-4

DO - 10.1016/0014-5793(89)80181-4

M3 - Article

C2 - 2924916

AN - SCOPUS:0024535395

SN - 0014-5793

VL - 245

SP - 14

EP - 16

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

DNA polymerase α-DNA primase from human placenta Immunoaffinity purification and preliminary characterization

Abstract

Keywords

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