Abstract
Amino acid sequences deduced from rat complementary DNA clones encoding the insulin-like growth factor II(IGF-II) receptor closely resemble those of the bovine cation-independent mannose-6-phosphate receptor (Man-6-P receptor CI), suggesting they are identical structures. It is also shown that IGF-II receptors are adsorbed by immobilized pentamannosyl-6-phosphate and are specifically eluted with Man-6-P. Furthermore, Man-6-P specifically increases by about two times the apparent affinity of the purified rat placental receptor for 125I-labeled IGF-II. These results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P-containing proteins.
Original language | English (US) |
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Pages (from-to) | 1134-1137 |
Number of pages | 4 |
Journal | Science |
Volume | 239 |
Issue number | 4844 |
DOIs | |
State | Published - 1988 |
Externally published | Yes |
ASJC Scopus subject areas
- General