Kang, HT Bang, WK Yu, YG 2024-01-21T07:14:47Z 2024-01-21T07:14:47Z 2022-01-10 2004-03-31 1225-8687 https://pubs.kist.re.kr/handle/201004/137751 Angiostatin is a potent anti-angiogenic protein. To examine the angiostatin-interacting proteins, we used the display-cloning method with a T7 phage library presenting human cDNAs. The specific T7 phage clone that bound to the immobilized angiostatin was isolated, and a novel gene encoding the displayed polypeptide on the isolated T7 phage was identified. The displayed angiostatin-binding sequence was expressed in E. coli as a soluble protein and purified to homogeneity. This novel angiostatin-binding region interacted specifically to angiostatin with a dissociation constant of 3.4 x 10(-7) M. A sequence analysis showed that the identified sequence was a part of the large ORF of 1,998 amino acids, whose function has not yet been characterized. A Northern analysis indicated that the gene containing the angiostatin-binding sequence was expressed differentially in the developmental stages or cell types. English SPRINGER SINGAPORE PTE LTD PHAGE DISPLAY ANGIOGENESIS INHIBITOR ENDOTHELIAL-CELLS KRINGLE DOMAINS ATP SYNTHASE TUMOR-GROWTH SURFACE CANCER LIBRARY PLASMINOGEN Identification and characterization of a novel angiostatin-bindin protein by the display cloning method Article 1 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.37, no.2, pp.159 - 166 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY 37 2 159 166 scie scopus 000220550000005 2-s2.0-2342521850 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article PHAGE DISPLAY ANGIOGENESIS INHIBITOR ENDOTHELIAL-CELLS KRINGLE DOMAINS ATP SYNTHASE TUMOR-GROWTH SURFACE CANCER LIBRARY PLASMINOGEN angiogenesis angiostatin angiostatin-binding protein display cloning T7 phage