@article {Buchko:2001:0929-8665:357,
title = "Hydroxyapatite Elution Behavior of Human Nucleotide Excision Repair Protein XPA and Fragments of XPA",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2001",
volume = "8",
number = "5",
publication date ="2001-10-01T00:00:00",
pages = "357-365",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2001/00000008/00000005/art00004",
doi = "doi:10.2174/0929866013409300",
keyword = "XPA gene, Nucleotide excision repair (NER), REPAIR PROTEIN XPA",
author = "Buchko, Garry W. and Kennedy, Michael A.",
abstract = "The hydroxyapatite elution behavior of 3 fragments of human XPA (M98-F219 = XPA-MBD M59-F219 = XPA-EM M59-M273 = XPA-deltaN58) and full-length human XPA containing a 6-residue, N-terminal histidine tag (h6-XPA) are described. With increasing concentration of potassium phosphate the proteins elute in the order: XPA-EM, XPA-MBD, XPA-deltaN58, and h6-XPA. If hydroxyapatite affinity is related to DNA-binding affinity, then h6-XPA and XPA-deltaN58 may bind DNA more tightly than XPA-MBD and XPA-EM.",
}