Erythropoiesis Stimulating Factors

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

doi:10.1111/j.1600-0609.1971.tb01974.x

Erythropoiesis Stimulating Factors

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

Pulmonary Disease

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

11 Scopus citations

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 language	English (US)
Pages (from-to)	200-209
Number of pages	10
Journal	Scandinavian Journal of Haematology
Volume	8
Issue number	3
DOIs	https://doi.org/10.1111/j.1600-0609.1971.tb01974.x
State	Published - Jul 1971

ASJC Scopus subject areas

Hematology

Access to Document

10.1111/j.1600-0609.1971.tb01974.x

Cite this

@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, {Russel R.} and Welch, {Emily T.} and Edward Gardner and Wright, {Claude‐Starr ‐S} and Smith, {Linda L.}",

year = "1971",

month = jul,

doi = "10.1111/j.1600-0609.1971.tb01974.x",

language = "English (US)",

volume = "8",

pages = "200--209",

journal = "Scandinavian Journal of Haematology",

issn = "0036-553X",

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, Russel R.

AU - Welch, Emily T.

AU - Gardner, Edward

AU - Wright, Claude‐Starr ‐S

AU - Smith, Linda L.

PY - 1971/7

Y1 - 1971/7

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

SN - 0036-553X

VL - 8

SP - 200

EP - 209

JO - Scandinavian Journal of Haematology

JF - Scandinavian Journal of Haematology

IS - 3

ER -

Erythropoiesis Stimulating Factors

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this