Erythropoiesis Stimulating Factors

Jasper P. Lewis, Dorothy A. Alford, W. Aubrey Neal, Russell R Moores, Emily T. Welch, Edward Gardner, Claude‐Starr ‐S Wright, Linda L. Smith

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

A urine concentrate of erythropoietin, obtained by chromatography on diethylamino‐ethyl (DEAE)‐cellulose, contained regulators of erythropoiesis that could be fractionated by selective membrane permeability. Two erythropoiesis stimulating factors (ESF) were obtained after exhaustive dialysis, one that diffused through the membrane and one in the retentate. A biochemical study of the ESF in the diffusate showed no appreciable sialic acid or fucose, a trace of hexosamine and a relatively small amount of protein. The remainder of the complex appeared to be an adrenocorticosteroid(s). The protein appeared to be a fragment of a glycoprotein. After exhaustive dialysis the retentate‐ESF had the characteristics of an ESF‐generating factor. The optimum pH for activity was about 7.4. It is suggested that an ESF(s) remains inactive when bound to a glycoprotein such as α1‐acid glycoprotein or the corticosteroid‐binding globulin. A role of an ESF‐generating factor would be to act on the complex to produce a fragment of the glycoprotein steroid complex, thereby activating the hormone.

Original languageEnglish (US)
Pages (from-to)200-209
Number of pages10
JournalScandinavian Journal of Haematology
Volume8
Issue number3
DOIs
StatePublished - Jan 1 1971

Fingerprint

Erythropoiesis
Glycoproteins
Dialysis
Hexosamines
Fucose
Membranes
Globulins
N-Acetylneuraminic Acid
Erythropoietin
Cellulose
Chromatography
Permeability
Proteins
Steroids
Urine
Hormones

ASJC Scopus subject areas

  • Hematology

Cite this

Lewis, J. P., Alford, D. A., Neal, W. A., Moores, R. R., Welch, E. T., Gardner, E., ... Smith, L. L. (1971). Erythropoiesis Stimulating Factors. Scandinavian Journal of Haematology, 8(3), 200-209. https://doi.org/10.1111/j.1600-0609.1971.tb01974.x

Erythropoiesis Stimulating Factors. / Lewis, Jasper P.; Alford, Dorothy A.; Neal, W. Aubrey; Moores, Russell R; Welch, Emily T.; Gardner, Edward; Wright, Claude‐Starr ‐S; Smith, Linda L.

In: Scandinavian Journal of Haematology, Vol. 8, No. 3, 01.01.1971, p. 200-209.

Research output: Contribution to journalArticle

Lewis, JP, Alford, DA, Neal, WA, Moores, RR, Welch, ET, Gardner, E, Wright, CSS & Smith, LL 1971, 'Erythropoiesis Stimulating Factors', Scandinavian Journal of Haematology, vol. 8, no. 3, pp. 200-209. https://doi.org/10.1111/j.1600-0609.1971.tb01974.x
Lewis JP, Alford DA, Neal WA, Moores RR, Welch ET, Gardner E et al. Erythropoiesis Stimulating Factors. Scandinavian Journal of Haematology. 1971 Jan 1;8(3):200-209. https://doi.org/10.1111/j.1600-0609.1971.tb01974.x
Lewis, Jasper P. ; Alford, Dorothy A. ; Neal, W. Aubrey ; Moores, Russell R ; Welch, Emily T. ; Gardner, Edward ; Wright, Claude‐Starr ‐S ; Smith, Linda L. / Erythropoiesis Stimulating Factors. In: Scandinavian Journal of Haematology. 1971 ; Vol. 8, No. 3. pp. 200-209.
@article{f71df895eeef4c608b30484f885691c3,
title = "Erythropoiesis Stimulating Factors",
abstract = "A urine concentrate of erythropoietin, obtained by chromatography on diethylamino‐ethyl (DEAE)‐cellulose, contained regulators of erythropoiesis that could be fractionated by selective membrane permeability. Two erythropoiesis stimulating factors (ESF) were obtained after exhaustive dialysis, one that diffused through the membrane and one in the retentate. A biochemical study of the ESF in the diffusate showed no appreciable sialic acid or fucose, a trace of hexosamine and a relatively small amount of protein. The remainder of the complex appeared to be an adrenocorticosteroid(s). The protein appeared to be a fragment of a glycoprotein. After exhaustive dialysis the retentate‐ESF had the characteristics of an ESF‐generating factor. The optimum pH for activity was about 7.4. It is suggested that an ESF(s) remains inactive when bound to a glycoprotein such as α1‐acid glycoprotein or the corticosteroid‐binding globulin. A role of an ESF‐generating factor would be to act on the complex to produce a fragment of the glycoprotein steroid complex, thereby activating the hormone.",
author = "Lewis, {Jasper P.} and Alford, {Dorothy A.} and Neal, {W. Aubrey} and Moores, {Russell R} and Welch, {Emily T.} and Edward Gardner and Wright, {Claude‐Starr ‐S} and Smith, {Linda L.}",
year = "1971",
month = "1",
day = "1",
doi = "10.1111/j.1600-0609.1971.tb01974.x",
language = "English (US)",
volume = "8",
pages = "200--209",
journal = "European Journal of Haematology",
issn = "0902-4441",
publisher = "Wiley-Blackwell",
number = "3",

}

TY - JOUR

T1 - Erythropoiesis Stimulating Factors

AU - Lewis, Jasper P.

AU - Alford, Dorothy A.

AU - Neal, W. Aubrey

AU - Moores, Russell R

AU - Welch, Emily T.

AU - Gardner, Edward

AU - Wright, Claude‐Starr ‐S

AU - Smith, Linda L.

PY - 1971/1/1

Y1 - 1971/1/1

N2 - A urine concentrate of erythropoietin, obtained by chromatography on diethylamino‐ethyl (DEAE)‐cellulose, contained regulators of erythropoiesis that could be fractionated by selective membrane permeability. Two erythropoiesis stimulating factors (ESF) were obtained after exhaustive dialysis, one that diffused through the membrane and one in the retentate. A biochemical study of the ESF in the diffusate showed no appreciable sialic acid or fucose, a trace of hexosamine and a relatively small amount of protein. The remainder of the complex appeared to be an adrenocorticosteroid(s). The protein appeared to be a fragment of a glycoprotein. After exhaustive dialysis the retentate‐ESF had the characteristics of an ESF‐generating factor. The optimum pH for activity was about 7.4. It is suggested that an ESF(s) remains inactive when bound to a glycoprotein such as α1‐acid glycoprotein or the corticosteroid‐binding globulin. A role of an ESF‐generating factor would be to act on the complex to produce a fragment of the glycoprotein steroid complex, thereby activating the hormone.

AB - A urine concentrate of erythropoietin, obtained by chromatography on diethylamino‐ethyl (DEAE)‐cellulose, contained regulators of erythropoiesis that could be fractionated by selective membrane permeability. Two erythropoiesis stimulating factors (ESF) were obtained after exhaustive dialysis, one that diffused through the membrane and one in the retentate. A biochemical study of the ESF in the diffusate showed no appreciable sialic acid or fucose, a trace of hexosamine and a relatively small amount of protein. The remainder of the complex appeared to be an adrenocorticosteroid(s). The protein appeared to be a fragment of a glycoprotein. After exhaustive dialysis the retentate‐ESF had the characteristics of an ESF‐generating factor. The optimum pH for activity was about 7.4. It is suggested that an ESF(s) remains inactive when bound to a glycoprotein such as α1‐acid glycoprotein or the corticosteroid‐binding globulin. A role of an ESF‐generating factor would be to act on the complex to produce a fragment of the glycoprotein steroid complex, thereby activating the hormone.

UR - http://www.scopus.com/inward/record.url?scp=0014989083&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014989083&partnerID=8YFLogxK

U2 - 10.1111/j.1600-0609.1971.tb01974.x

DO - 10.1111/j.1600-0609.1971.tb01974.x

M3 - Article

C2 - 5093997

AN - SCOPUS:0014989083

VL - 8

SP - 200

EP - 209

JO - European Journal of Haematology

JF - European Journal of Haematology

SN - 0902-4441

IS - 3

ER -