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

Research output: Contribution to journalArticle

20 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)561-567
Number of pages7
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume92
Issue number3
DOIs
StatePublished - Jan 1 1989

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Insulin-Like Growth Factor Binding Proteins
Sus scrofa
Purification
Swine
Acids
Serum
Insulin-Like Growth Factor I
Plasma (human)
Insulin-Like Growth Factor II
Sequence Homology
Rats
Polyacrylamide Gel Electrophoresis
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

Cite this

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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.",
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Purification of the serum acid-stable insulin-like growth factor binding protein from the pig (Sus scrofa). / Walton, Paul E.; Baxter, Robert C.; Burleigh, B. Dan; Etherton, Terry D.

In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 92, No. 3, 01.01.1989, p. 561-567.

Research output: Contribution to journalArticle

TY - JOUR

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 - 1989/1/1

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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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