NATURAL AND SYNTHETIC FORMS OF INSULIN-LIKE GROWTH FACTOR-I (IGF-1) AND THE POTENT DERIVATIVE, DESTRIPEPTIDE IGF-1 - BIOLOGICAL-ACTIVITIES AND RECEPTOR-BINDING
NATURAL AND SYNTHETIC FORMS OF INSULIN-LIKE GROWTH FACTOR-I (IGF-1) AND THE POTENT DERIVATIVE, DESTRIPEPTIDE IGF-1 - BIOLOGICAL-ACTIVITIES AND RECEPTOR-BINDING
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DOI：
10.1016/0006-291x(87)90380-9
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发表时间：
1987-12-16
影响因子：
3.1
通讯作者：
WALLACE, JC
中科院分区：
文献类型：
--
作者：
BALLARD, FJ;FRANCIS, GL;WALLACE, JC
胰岛素样生长因子-1 (IGF-1)，无论是重组的、化学合成的还是从牛初乳中纯化的，在以IGF-1或胰岛素样生长因子-2 （IGF-2）作为放射配体的放射受体试验中都具有相同的效力，并且具有刺激L6成肌细胞蛋白质合成的能力。在蛋白质合成生物测定中，n端截断的IGF-1去条肽衍生物的效力大约是IGF-1的7倍。从牛初乳中纯化的肽与化学合成的肽同样具有这种增强的活性。截断形式的更高效力与竞争IGF-1与L6成肌细胞结合的能力增加无关。
Insulin-like growth factor-1 (IGF-1), whether recombinant, chemically-synthesised or purified from bovine colostrum, was equipotent in radioreceptor assays with IGF-1 or insulin-like growth factor-2 (IGF-2) as radioligand as well as in its ability to stimulate protein synthesis in L6 myoblasts. The N-terminal truncated, destripeptide derivative of IGF-1 was approximately 7 times more potent than IGF-1 in the protein synthesis bioassay. This increased activity occurred equally with the peptide purified from bovine colostrum as with chemically-synthesized material. The higher potency of the truncated form was not associated with an increased ability to compete for IGF-1 binding to L6 myoblasts.