TY - JOUR
T1 - Detection of glycosylated growth hormone-binding proteins in rat serum
AU - Haldosén, Lars Arne
AU - Gustafsson, Jan Åke
N1 - Funding Information:
This work was supported by grants from the Swedish Medical Research Council (B89-03X-04807-06C) and the Swedish Society of Medicine. The expert technical assistance of Mrs. Lena MSller and Ms. Marie Jernberger is gratefully acknowledged.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1990/1/22
Y1 - 1990/1/22
N2 - Affinity cross-linking technique revealed the presence of three growth hormone-binding proteins (GHBP) in dealbuminized rat serum. The apparent molecular weights, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were 52,000, 44,000 and 39,000. By use of carbohydrate chain cleaving enzymes it was found that the binding proteins contain N-linked complex carbohydrate chains, representing 8000, 4000 and 5000 in apparent molecular weight, respectively. Gel permeation chromatography and sucrose density gradient centrifugation revealed a growth hormone-binding entity with Stoke's radius 94.5 Å (±2.8, n = 5) and an s-value of 10.8 S (±0.31, n = 5). The molecular weight could be calculated to 413,000. Both for gel chromatography and sucrose density gradient experiments unlabelled growth hormone reduced the radioactive peaks from 0 to 50%. The relation of this binding entity to the GHBP's described with affinity cross-linking technique and the nature of this binding entity is at present unclear. No serum binding protein(s) for prolactin was detected by affinity cross-linking technique, gel permeation chromatography or sucrose density gradient analysis.
AB - Affinity cross-linking technique revealed the presence of three growth hormone-binding proteins (GHBP) in dealbuminized rat serum. The apparent molecular weights, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were 52,000, 44,000 and 39,000. By use of carbohydrate chain cleaving enzymes it was found that the binding proteins contain N-linked complex carbohydrate chains, representing 8000, 4000 and 5000 in apparent molecular weight, respectively. Gel permeation chromatography and sucrose density gradient centrifugation revealed a growth hormone-binding entity with Stoke's radius 94.5 Å (±2.8, n = 5) and an s-value of 10.8 S (±0.31, n = 5). The molecular weight could be calculated to 413,000. Both for gel chromatography and sucrose density gradient experiments unlabelled growth hormone reduced the radioactive peaks from 0 to 50%. The relation of this binding entity to the GHBP's described with affinity cross-linking technique and the nature of this binding entity is at present unclear. No serum binding protein(s) for prolactin was detected by affinity cross-linking technique, gel permeation chromatography or sucrose density gradient analysis.
KW - (Rat)
KW - Binding protein
KW - Growth hormone
KW - Serum
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U2 - 10.1016/0303-7207(90)90192-B
DO - 10.1016/0303-7207(90)90192-B
M3 - Article
C2 - 2311824
AN - SCOPUS:0025037562
VL - 68
SP - 187
EP - 194
JO - Molecular and cellular endocrinology
JF - Molecular and cellular endocrinology
SN - 0303-7207
IS - 2-3
ER -