Purification of the serum acid-stable insulin-like growth factor binding protein from the pig (Sus scrofa)

Paul E. Walton; Robert C. Baxter; B. Dan Burleigh; Terry D. Etherton

doi:10.1016/0305-0491(89)90132-6

Purification of the serum acid-stable insulin-like growth factor binding protein from the pig (Sus scrofa)

Paul E. Walton, Robert C. Baxter, B. Dan Burleigh, Terry D. Etherton

Animal Science

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

1. 1. An acid-stable IGF binding protein was isolated and purified from porcine serum. 2. 2. The protein comprised two major species with M_rs of 45 and 41 kDa determined using SDS-PAGE under reducing conditions. 3. 3. The IGFBP preparation specifically bound both IGF-I and II. 4. 4. Four distinct protein bands (M_rs of 23, 45, 50 and 75 kDa) in the porcine IGFBP preparation specifically bound radiolabelled IGF-I. 5. 5. The porcine IGFBP exhibited sequence homology with IGFBPs from human plasma and rat serum. 6. 6. This is the first report of the purification and characterization of the acid-stable IGFBP from porcine serum.

Original language	English (US)
Pages (from-to)	561-567
Number of pages	7
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	92
Issue number	3
DOIs	https://doi.org/10.1016/0305-0491(89)90132-6
State	Published - 1989

All Science Journal Classification (ASJC) codes

Biochemistry
Physiology
Molecular Biology

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title = "Purification of the serum acid-stable insulin-like growth factor binding protein from the pig (Sus scrofa)",

abstract = "1. 1. An acid-stable IGF binding protein was isolated and purified from porcine serum. 2. 2. The protein comprised two major species with Mrs of 45 and 41 kDa determined using SDS-PAGE under reducing conditions. 3. 3. The IGFBP preparation specifically bound both IGF-I and II. 4. 4. Four distinct protein bands (Mrs of 23, 45, 50 and 75 kDa) in the porcine IGFBP preparation specifically bound radiolabelled IGF-I. 5. 5. The porcine IGFBP exhibited sequence homology with IGFBPs from human plasma and rat serum. 6. 6. This is the first report of the purification and characterization of the acid-stable IGFBP from porcine serum.",

author = "Walton, {Paul E.} and Baxter, {Robert C.} and Burleigh, {B. Dan} and Etherton, {Terry D.}",

year = "1989",

doi = "10.1016/0305-0491(89)90132-6",

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T1 - Purification of the serum acid-stable insulin-like growth factor binding protein from the pig (Sus scrofa)

AU - Walton, Paul E.

AU - Baxter, Robert C.

AU - Burleigh, B. Dan

AU - Etherton, Terry D.

PY - 1989

Y1 - 1989

N2 - 1. 1. An acid-stable IGF binding protein was isolated and purified from porcine serum. 2. 2. The protein comprised two major species with Mrs of 45 and 41 kDa determined using SDS-PAGE under reducing conditions. 3. 3. The IGFBP preparation specifically bound both IGF-I and II. 4. 4. Four distinct protein bands (Mrs of 23, 45, 50 and 75 kDa) in the porcine IGFBP preparation specifically bound radiolabelled IGF-I. 5. 5. The porcine IGFBP exhibited sequence homology with IGFBPs from human plasma and rat serum. 6. 6. This is the first report of the purification and characterization of the acid-stable IGFBP from porcine serum.

AB - 1. 1. An acid-stable IGF binding protein was isolated and purified from porcine serum. 2. 2. The protein comprised two major species with Mrs of 45 and 41 kDa determined using SDS-PAGE under reducing conditions. 3. 3. The IGFBP preparation specifically bound both IGF-I and II. 4. 4. Four distinct protein bands (Mrs of 23, 45, 50 and 75 kDa) in the porcine IGFBP preparation specifically bound radiolabelled IGF-I. 5. 5. The porcine IGFBP exhibited sequence homology with IGFBPs from human plasma and rat serum. 6. 6. This is the first report of the purification and characterization of the acid-stable IGFBP from porcine serum.

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JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

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ER -

Purification of the serum acid-stable insulin-like growth factor binding protein from the pig (Sus scrofa)

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