scholarly journals Detection of the growth fraction in colorectal tumours by a monoclonal antibody against DNA polymerase α

1990 ◽  
Vol 61 (3) ◽  
pp. 390-393 ◽  
Author(s):  
A Yamaguchi ◽  
S Takegawa ◽  
T Ishida ◽  
G Nishimura ◽  
M Kato ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Dna Polymerase ◽  
Growth Fraction ◽  
Dna Polymerase Α ◽  
Colorectal Tumours

DNA Polymerase-Associated Lectin (DPAL) and Its Binding to the Galactose-Containing Glycoconjugate of the Replication Complex

1999 ◽  
Vol 19 (5) ◽  
pp. 433-447
Author(s):  
Thomas J. Kelley ◽  
Tara St. Amand ◽  
Jeremy M. Groll ◽  
Satyajit Ray ◽  
Subhash Basu
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Dna Polymerase ◽  
Recombinant Dna ◽  
Cultured Cells ◽  
Polyclonal Antibodies ◽  
Immunoblot Analysis ◽  
Post Translational Modification ◽  
Human Neuroblastoma ◽  
Dna Polymerase Α

The highly purified DNA Pol-α from rat prostate tumor (PA-3) and human neuroblastoma (IMR-32) cells appeared to be inhibited by Ricin (RCA-II), and Con-A. Loss of activity (40 to 60%) of a specific form of DNA polymerase from IMR-32 was observed when the cells were treated with tunicamycin [Bhattacharya, P. and Basu, S. (1982) Proc. Natl. Acad. Sci., USA79:1488–1492]. Binding of ConA and RCA to human recombinant DNA polymerase-α showed a specific labile site in the N-terminus [Hsi et al.. (1990) Nucleic Acid Res.18:6231–6237]. The catalytic polypeptide, DNA polymerase-α of eukaryotic origin, was isolated from developing tissues or cultured cells as a family of 180 to 120 kDa polypeptides, perhaps derived from a single primary structure. Immunoblot analysis with a monoclonal antibody (SJK-237-71) indicated that the lower molecular weight polypeptides resulted from either proteolytic cleavage of post-translational modification after specific cleavages. Present results suggest DNA polymerase-α from embryonic chicken brain (ECB) contains an α-galactose-binding subunit which may be involved in developmental regulation of the enzyme. It was shown before that the catalytic subunit of DNA polymerase-α reduces from 186 kDa in 11-day-old ECB to 120 kDa in 19-day-old ECB [Ray, S. et al. Cell Growth and Differentiation2:567–573] by the treatment with methyl-α-galactose. The low molecular weight DNA polymerase activity (120 kDa) can be reconstituted to high molecular weight (Mr = 186 kDa) with an α-galactose binding, 56 kDa lectin-like protein. Polyclonal antibodies raised against the purified lectin were able to precipitate DNA. Pol-α as determined by immunostaining with the polymerase-α-specific monoclonal antibody SJK 132-20, suggesting this is a DNA polymerase associated-lectin (DPAL). RCA-II and GS-I-Sepharose 4B chromatographies resulted in significant purification of DNA-α and a complete separation of polymerase complex and primase.

scholarly journals Characterization of a Mr= 56,000 polypeptide associated with 10S DNA polymerase α purified from calf thymus using monoclonal antibody

1985 ◽  
Vol 13 (18) ◽  
pp. 6635-6649 ◽  
Author(s):  
Shigeo Masaki ◽  
Katsuyuki Tamai ◽  
Rika Suzuki ◽  
Kazushi Tanabe ◽  
Taijo Takahashi ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Dna Polymerase ◽  
Dna Polymerase Α ◽  
Calf Thymus

Monoclonal antibody specific for chicken DNA polymerase α associated with DNA primase

1985 ◽  
Vol 132 (1) ◽  
pp. 210-216 ◽  
Author(s):  
Fumiko Hirose ◽  
Padmini Kedar ◽  
Taijo Takahashi ◽  
Akio Matsukage
Keyword(s):  
Monoclonal Antibody ◽  
Dna Polymerase ◽  
Dna Primase ◽  
Dna Polymerase Α
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