Characterization of human alpha fetoprotein charge microheterogeneity during fetal development

Brooks Allen Keel, Robin L. Harms, Juan A. Leal, Sechin Cho

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Aliquotes of human amniotic fluid (AF), fetal serum (FS), and cord blood (CB) were obtained as by‐products of routine clinical diagnostic procedures at term or in the second trimester of pregnancy. When samples of CB were applied to a pH 5.5‐4 chromatofocusing gradient, three isoforms of AFP could be resolved; a pl 4.57 form (isoform IA, 52% AFP), a pl 4.27 form (isoform IB, 43% AFP), and one species that was bound to the column but could be eluted with 1.0 M NaCl (isoform II, pl<4.00, 5% AFP). Term AF displayed a profile similar to that observed in term CB. When samples of 15–20‐week gestation AF were chromatofocused, the immunoreactive AFP recovered was distributed between isoform IA and IB (60%) and isoform II (40%). FS and AF obtained from same pregnancy (23–26 weeks) displayed an identical chromatofocusing profile. Aliquotes of AF subjected to conA revealed 83% reactive variants compared with >95% reactive variants for CB. FS displayed a conA profile identical to CB. When individual CB charge isoforms were isolated and subjected to conA analysis, >97% of the AFP bound to conA. In contrast, when AFP isoforms IA and IB were isolated from midgestation AF, approximately 22% of the AFP did not bind to the lectin while 100% of isolated AFP isoform II eluted as the reactive variant. These data suggest that human AFP exists as at least three charge and two lectin variants and that the charge profile may change during fetal development.

Original languageEnglish (US)
Pages (from-to)281-287
Number of pages7
JournalMolecular Reproduction and Development
Volume27
Issue number4
DOIs
StatePublished - Jan 1 1990

Fingerprint

Fetal Development
Fetal Blood
Protein Isoforms
Amniotic Fluid
Lectins
Second Pregnancy Trimester
human AFP protein
Serum

Keywords

  • AFP
  • Cord blood
  • Fetal serum

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology
  • Cell Biology

Cite this

Characterization of human alpha fetoprotein charge microheterogeneity during fetal development. / Keel, Brooks Allen; Harms, Robin L.; Leal, Juan A.; Cho, Sechin.

In: Molecular Reproduction and Development, Vol. 27, No. 4, 01.01.1990, p. 281-287.

Research output: Contribution to journalArticle

@article{fe04a32efb644d219537587316b5b4b0,
title = "Characterization of human alpha fetoprotein charge microheterogeneity during fetal development",
abstract = "Aliquotes of human amniotic fluid (AF), fetal serum (FS), and cord blood (CB) were obtained as by‐products of routine clinical diagnostic procedures at term or in the second trimester of pregnancy. When samples of CB were applied to a pH 5.5‐4 chromatofocusing gradient, three isoforms of AFP could be resolved; a pl 4.57 form (isoform IA, 52{\%} AFP), a pl 4.27 form (isoform IB, 43{\%} AFP), and one species that was bound to the column but could be eluted with 1.0 M NaCl (isoform II, pl<4.00, 5{\%} AFP). Term AF displayed a profile similar to that observed in term CB. When samples of 15–20‐week gestation AF were chromatofocused, the immunoreactive AFP recovered was distributed between isoform IA and IB (60{\%}) and isoform II (40{\%}). FS and AF obtained from same pregnancy (23–26 weeks) displayed an identical chromatofocusing profile. Aliquotes of AF subjected to conA revealed 83{\%} reactive variants compared with >95{\%} reactive variants for CB. FS displayed a conA profile identical to CB. When individual CB charge isoforms were isolated and subjected to conA analysis, >97{\%} of the AFP bound to conA. In contrast, when AFP isoforms IA and IB were isolated from midgestation AF, approximately 22{\%} of the AFP did not bind to the lectin while 100{\%} of isolated AFP isoform II eluted as the reactive variant. These data suggest that human AFP exists as at least three charge and two lectin variants and that the charge profile may change during fetal development.",
keywords = "AFP, Cord blood, Fetal serum",
author = "Keel, {Brooks Allen} and Harms, {Robin L.} and Leal, {Juan A.} and Sechin Cho",
year = "1990",
month = "1",
day = "1",
doi = "10.1002/mrd.1080270402",
language = "English (US)",
volume = "27",
pages = "281--287",
journal = "Molecular Reproduction and Development",
issn = "1040-452X",
publisher = "Wiley-Liss Inc.",
number = "4",

}

TY - JOUR

T1 - Characterization of human alpha fetoprotein charge microheterogeneity during fetal development

AU - Keel, Brooks Allen

AU - Harms, Robin L.

AU - Leal, Juan A.

AU - Cho, Sechin

PY - 1990/1/1

Y1 - 1990/1/1

N2 - Aliquotes of human amniotic fluid (AF), fetal serum (FS), and cord blood (CB) were obtained as by‐products of routine clinical diagnostic procedures at term or in the second trimester of pregnancy. When samples of CB were applied to a pH 5.5‐4 chromatofocusing gradient, three isoforms of AFP could be resolved; a pl 4.57 form (isoform IA, 52% AFP), a pl 4.27 form (isoform IB, 43% AFP), and one species that was bound to the column but could be eluted with 1.0 M NaCl (isoform II, pl<4.00, 5% AFP). Term AF displayed a profile similar to that observed in term CB. When samples of 15–20‐week gestation AF were chromatofocused, the immunoreactive AFP recovered was distributed between isoform IA and IB (60%) and isoform II (40%). FS and AF obtained from same pregnancy (23–26 weeks) displayed an identical chromatofocusing profile. Aliquotes of AF subjected to conA revealed 83% reactive variants compared with >95% reactive variants for CB. FS displayed a conA profile identical to CB. When individual CB charge isoforms were isolated and subjected to conA analysis, >97% of the AFP bound to conA. In contrast, when AFP isoforms IA and IB were isolated from midgestation AF, approximately 22% of the AFP did not bind to the lectin while 100% of isolated AFP isoform II eluted as the reactive variant. These data suggest that human AFP exists as at least three charge and two lectin variants and that the charge profile may change during fetal development.

AB - Aliquotes of human amniotic fluid (AF), fetal serum (FS), and cord blood (CB) were obtained as by‐products of routine clinical diagnostic procedures at term or in the second trimester of pregnancy. When samples of CB were applied to a pH 5.5‐4 chromatofocusing gradient, three isoforms of AFP could be resolved; a pl 4.57 form (isoform IA, 52% AFP), a pl 4.27 form (isoform IB, 43% AFP), and one species that was bound to the column but could be eluted with 1.0 M NaCl (isoform II, pl<4.00, 5% AFP). Term AF displayed a profile similar to that observed in term CB. When samples of 15–20‐week gestation AF were chromatofocused, the immunoreactive AFP recovered was distributed between isoform IA and IB (60%) and isoform II (40%). FS and AF obtained from same pregnancy (23–26 weeks) displayed an identical chromatofocusing profile. Aliquotes of AF subjected to conA revealed 83% reactive variants compared with >95% reactive variants for CB. FS displayed a conA profile identical to CB. When individual CB charge isoforms were isolated and subjected to conA analysis, >97% of the AFP bound to conA. In contrast, when AFP isoforms IA and IB were isolated from midgestation AF, approximately 22% of the AFP did not bind to the lectin while 100% of isolated AFP isoform II eluted as the reactive variant. These data suggest that human AFP exists as at least three charge and two lectin variants and that the charge profile may change during fetal development.

KW - AFP

KW - Cord blood

KW - Fetal serum

UR - http://www.scopus.com/inward/record.url?scp=0025221776&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025221776&partnerID=8YFLogxK

U2 - 10.1002/mrd.1080270402

DO - 10.1002/mrd.1080270402

M3 - Article

C2 - 1702295

AN - SCOPUS:0025221776

VL - 27

SP - 281

EP - 287

JO - Molecular Reproduction and Development

JF - Molecular Reproduction and Development

SN - 1040-452X

IS - 4

ER -