The α and β Chains of Human Platelet Glycoprotein Ib are Both Transmembrane Proteins Containing a Leucine-Rich Amino Acid Sequence

The primary structure of the β chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence analysis. A λ phage cDNA expression library prepared from human erythroleukemia cells (HEL cells) was s...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1988-04, Vol.85 (7), p.2135-2139
Hauptverfasser: Lopez, Jose A., Chung, Dominic W., Fujikawa, Kazuo, Hagen, Frederick S., Davie, Earl W., Roth, Gerald J.
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container_end_page 2139
container_issue 7
container_start_page 2135
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 85
creator Lopez, Jose A.
Chung, Dominic W.
Fujikawa, Kazuo
Hagen, Frederick S.
Davie, Earl W.
Roth, Gerald J.
description The primary structure of the β chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence analysis. A λ phage cDNA expression library prepared from human erythroleukemia cells (HEL cells) was screened with a radiolabeled affinity-purified rabbit polyclonal antibody to the β chain of GPIb. Eighteen positive clones were isolated and plaque-purified and the nucleotide sequences of three were determined. The composite sequence spanned 968 nucleotides and included a 5′ untranslated region of 22 nucleotides, an open reading frame of 618 nucleotides encoding a signal peptide of 28 amino acids and a mature protein of 181 amino acids, a stop codon, and a 3′ noncoding region of 307 nucleotides. The 3′ noncoding sequence also contained a polyadenylylation signal (AATAAA) 14 nucleotides upstream from the poly(A) tail of 18 nucleotides. Edman degradation of the intact β chain and of peptides produced by chemical cleavage yielded amino acid sequences spanning 76 residues that were identical to those predicted from the cDNA. The amino-terminal region of the β chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the α chain of GPIb and nine tandem repeats in leucine-rich α 2-glycoprotein. The leucine-rich sequence in the β chain of GPIb is flanked on both sides by amino acid sequences that are similar to those flanking the leucine-rich tandem repeats of the α chain of GPIb and leucine-rich α 2-glycoprotein. The amino-terminal region of the β chain of GPIb is followed by a transmembrane segment of 25 amino acids and an intracellular segment of 34 amino acids at the carboxyl terminus of the protein. The intracellular segment contains an unpaired cysteine and two potential sites for phosphorylation by cAMP-dependent protein kinase.
doi_str_mv 10.1073/pnas.85.7.2135
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A λ phage cDNA expression library prepared from human erythroleukemia cells (HEL cells) was screened with a radiolabeled affinity-purified rabbit polyclonal antibody to the β chain of GPIb. Eighteen positive clones were isolated and plaque-purified and the nucleotide sequences of three were determined. The composite sequence spanned 968 nucleotides and included a 5′ untranslated region of 22 nucleotides, an open reading frame of 618 nucleotides encoding a signal peptide of 28 amino acids and a mature protein of 181 amino acids, a stop codon, and a 3′ noncoding region of 307 nucleotides. The 3′ noncoding sequence also contained a polyadenylylation signal (AATAAA) 14 nucleotides upstream from the poly(A) tail of 18 nucleotides. Edman degradation of the intact β chain and of peptides produced by chemical cleavage yielded amino acid sequences spanning 76 residues that were identical to those predicted from the cDNA. The amino-terminal region of the β chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the α chain of GPIb and nine tandem repeats in leucine-rich α 2-glycoprotein. The leucine-rich sequence in the β chain of GPIb is flanked on both sides by amino acid sequences that are similar to those flanking the leucine-rich tandem repeats of the α chain of GPIb and leucine-rich α 2-glycoprotein. The amino-terminal region of the β chain of GPIb is followed by a transmembrane segment of 25 amino acids and an intracellular segment of 34 amino acids at the carboxyl terminus of the protein. 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Psychology ; GENE REGULATION ; GENES ; GLUCOPROTEINS ; GLYCOPROTEINS ; HALIDES ; HALOGEN COMPOUNDS ; HEMIC DISEASES ; Humans ; HYBRIDIZATION ; IMMUNE SYSTEM DISEASES ; INORGANIC PHOSPHORS ; INTERMEDIATE MASS NUCLEI ; IODIDES ; IODINE 125 ; IODINE COMPOUNDS ; IODINE ISOTOPES ; ISOTOPES ; LEUCINE ; Leucine - analysis ; LEUKEMIA ; LIGHT NUCLEI ; MATERIALS ; Molecular Sequence Data ; MOLECULAR STRUCTURE ; NEOPLASMS ; NUCLEI ; NUCLEIC ACIDS ; Nucleotide sequences ; Nucleotides ; ODD-EVEN NUCLEI ; ORGANIC ACIDS ; ORGANIC COMPOUNDS ; PATIENTS ; PHORBOL ESTERS ; PHOSPHORS ; Phosphorylation ; Platelet Membrane Glycoproteins - genetics ; Platelets ; PROTEINS ; RADIOISOTOPES ; RECOMBINANT DNA ; SACCHARIDES ; Sequence Homology, Nucleic Acid ; Sequencing ; SODIUM COMPOUNDS ; SODIUM IODIDES ; STRUCTURAL CHEMICAL ANALYSIS ; SULFUR 35 ; SULFUR ISOTOPES 550201 -- Biochemistry-- Tracer Techniques ; Tandem repeat sequences ; TUMOR CELLS</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1988-04, Vol.85 (7), p.2135-2139</ispartof><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-bb7e85665b50b417a6b3736fb32f7d7819ae95bb4376f9ca10f21c1ec9f52dde3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/85/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/31083$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/31083$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=7098910$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3353370$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6897468$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Lopez, Jose A.</creatorcontrib><creatorcontrib>Chung, Dominic W.</creatorcontrib><creatorcontrib>Fujikawa, Kazuo</creatorcontrib><creatorcontrib>Hagen, Frederick S.</creatorcontrib><creatorcontrib>Davie, Earl W.</creatorcontrib><creatorcontrib>Roth, Gerald J.</creatorcontrib><title>The α and β Chains of Human Platelet Glycoprotein Ib are Both Transmembrane Proteins Containing a Leucine-Rich Amino Acid Sequence</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The primary structure of the β chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence analysis. A λ phage cDNA expression library prepared from human erythroleukemia cells (HEL cells) was screened with a radiolabeled affinity-purified rabbit polyclonal antibody to the β chain of GPIb. Eighteen positive clones were isolated and plaque-purified and the nucleotide sequences of three were determined. The composite sequence spanned 968 nucleotides and included a 5′ untranslated region of 22 nucleotides, an open reading frame of 618 nucleotides encoding a signal peptide of 28 amino acids and a mature protein of 181 amino acids, a stop codon, and a 3′ noncoding region of 307 nucleotides. The 3′ noncoding sequence also contained a polyadenylylation signal (AATAAA) 14 nucleotides upstream from the poly(A) tail of 18 nucleotides. Edman degradation of the intact β chain and of peptides produced by chemical cleavage yielded amino acid sequences spanning 76 residues that were identical to those predicted from the cDNA. The amino-terminal region of the β chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the α chain of GPIb and nine tandem repeats in leucine-rich α 2-glycoprotein. The leucine-rich sequence in the β chain of GPIb is flanked on both sides by amino acid sequences that are similar to those flanking the leucine-rich tandem repeats of the α chain of GPIb and leucine-rich α 2-glycoprotein. The amino-terminal region of the β chain of GPIb is followed by a transmembrane segment of 25 amino acids and an intracellular segment of 34 amino acids at the carboxyl terminus of the protein. The intracellular segment contains an unpaired cysteine and two potential sites for phosphorylation by cAMP-dependent protein kinase.</description><subject>ALKALI METAL COMPOUNDS</subject><subject>AMINO ACID SEQUENCE</subject><subject>AMINO ACIDS</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ANIMAL CELLS</subject><subject>ANTIBODIES</subject><subject>Base Sequence</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>BLOOD PLATELETS</subject><subject>BODY FLUIDS</subject><subject>CARBOHYDRATES</subject><subject>CARBOXYLIC ACIDS</subject><subject>CARCINOGENS</subject><subject>CLONING</subject><subject>Complementary DNA</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DISEASES</subject><subject>DNA</subject><subject>DNA - genetics</subject><subject>DNA HYBRIDIZATION</subject><subject>DNA SEQUENCING</subject><subject>DNA-CLONING</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>ELECTROPHORESIS</subject><subject>ESTERS</subject><subject>EVEN-ODD NUCLEI</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE REGULATION</subject><subject>GENES</subject><subject>GLUCOPROTEINS</subject><subject>GLYCOPROTEINS</subject><subject>HALIDES</subject><subject>HALOGEN COMPOUNDS</subject><subject>HEMIC DISEASES</subject><subject>Humans</subject><subject>HYBRIDIZATION</subject><subject>IMMUNE SYSTEM DISEASES</subject><subject>INORGANIC PHOSPHORS</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODIDES</subject><subject>IODINE 125</subject><subject>IODINE COMPOUNDS</subject><subject>IODINE ISOTOPES</subject><subject>ISOTOPES</subject><subject>LEUCINE</subject><subject>Leucine - analysis</subject><subject>LEUKEMIA</subject><subject>LIGHT NUCLEI</subject><subject>MATERIALS</subject><subject>Molecular Sequence Data</subject><subject>MOLECULAR STRUCTURE</subject><subject>NEOPLASMS</subject><subject>NUCLEI</subject><subject>NUCLEIC ACIDS</subject><subject>Nucleotide sequences</subject><subject>Nucleotides</subject><subject>ODD-EVEN NUCLEI</subject><subject>ORGANIC ACIDS</subject><subject>ORGANIC COMPOUNDS</subject><subject>PATIENTS</subject><subject>PHORBOL ESTERS</subject><subject>PHOSPHORS</subject><subject>Phosphorylation</subject><subject>Platelet Membrane Glycoproteins - genetics</subject><subject>Platelets</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>RECOMBINANT DNA</subject><subject>SACCHARIDES</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Sequencing</subject><subject>SODIUM COMPOUNDS</subject><subject>SODIUM IODIDES</subject><subject>STRUCTURAL CHEMICAL ANALYSIS</subject><subject>SULFUR 35</subject><subject>SULFUR ISOTOPES 550201 -- Biochemistry-- Tracer Techniques</subject><subject>Tandem repeat sequences</subject><subject>TUMOR CELLS</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u1DAUhSMEKkNhywIJyUKouwx2HMf2chhBW2kkKhjWlu3cMK4Se4gdie55IXiQPlM9yrR0xeouznfP_TlF8ZrgJcGcfth7HZeCLfmyIpQ9KRYES1I2tcRPiwXGFS9FXdXPixcxXmOMJRP4pDihlFHK8aL4vd0Buv2DtG_R7V-03mnnIwodupgG7dFVrxP0kNB5f2PDfgwJnEeXBukR0MeQdmg7ah8HGEyugK5mIqJ18ClbOf8DabSByToP5Vdnd2g1OB_QyroWfYOfE3gLL4tnne4jvDrW0-L750_b9UW5-XJ-uV5tSsuqOpXGcBCsaZhh2NSE68ZQTpvO0KrjLRdEapDMmJryppNWE9xVxBKwsmNV2wI9Ld7NviEmp6J1CezOBu_BJtUIyetGZOhshvK1eb2Y1OCihb7P94UpqjynFpXEGVzOoB1DjCN0aj-6QY83imB1yEYdslGCKa4O2eSGt0fnyQzQPuDHMLL-_qjraHXf5Y9aFx8wjqWQBD-yOdjfq4_HnP1PV93U9wl-pQy-mcHrmML4bx2CBaV3imi48g</recordid><startdate>19880401</startdate><enddate>19880401</enddate><creator>Lopez, Jose A.</creator><creator>Chung, Dominic W.</creator><creator>Fujikawa, Kazuo</creator><creator>Hagen, Frederick S.</creator><creator>Davie, Earl W.</creator><creator>Roth, Gerald J.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19880401</creationdate><title>The α and β Chains of Human Platelet Glycoprotein Ib are Both Transmembrane Proteins Containing a Leucine-Rich Amino Acid Sequence</title><author>Lopez, Jose A. ; Chung, Dominic W. ; Fujikawa, Kazuo ; Hagen, Frederick S. ; Davie, Earl W. ; Roth, Gerald J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c524t-bb7e85665b50b417a6b3736fb32f7d7819ae95bb4376f9ca10f21c1ec9f52dde3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>ALKALI METAL COMPOUNDS</topic><topic>AMINO ACID SEQUENCE</topic><topic>AMINO ACIDS</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ANIMAL CELLS</topic><topic>ANTIBODIES</topic><topic>Base Sequence</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL MATERIALS</topic><topic>BLOOD</topic><topic>BLOOD CELLS</topic><topic>BLOOD PLATELETS</topic><topic>BODY FLUIDS</topic><topic>CARBOHYDRATES</topic><topic>CARBOXYLIC ACIDS</topic><topic>CARCINOGENS</topic><topic>CLONING</topic><topic>Complementary DNA</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DISEASES</topic><topic>DNA</topic><topic>DNA - genetics</topic><topic>DNA HYBRIDIZATION</topic><topic>DNA SEQUENCING</topic><topic>DNA-CLONING</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>ELECTROPHORESIS</topic><topic>ESTERS</topic><topic>EVEN-ODD NUCLEI</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE REGULATION</topic><topic>GENES</topic><topic>GLUCOPROTEINS</topic><topic>GLYCOPROTEINS</topic><topic>HALIDES</topic><topic>HALOGEN COMPOUNDS</topic><topic>HEMIC DISEASES</topic><topic>Humans</topic><topic>HYBRIDIZATION</topic><topic>IMMUNE SYSTEM DISEASES</topic><topic>INORGANIC PHOSPHORS</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODIDES</topic><topic>IODINE 125</topic><topic>IODINE COMPOUNDS</topic><topic>IODINE ISOTOPES</topic><topic>ISOTOPES</topic><topic>LEUCINE</topic><topic>Leucine - analysis</topic><topic>LEUKEMIA</topic><topic>LIGHT NUCLEI</topic><topic>MATERIALS</topic><topic>Molecular Sequence Data</topic><topic>MOLECULAR STRUCTURE</topic><topic>NEOPLASMS</topic><topic>NUCLEI</topic><topic>NUCLEIC ACIDS</topic><topic>Nucleotide sequences</topic><topic>Nucleotides</topic><topic>ODD-EVEN NUCLEI</topic><topic>ORGANIC ACIDS</topic><topic>ORGANIC COMPOUNDS</topic><topic>PATIENTS</topic><topic>PHORBOL ESTERS</topic><topic>PHOSPHORS</topic><topic>Phosphorylation</topic><topic>Platelet Membrane Glycoproteins - genetics</topic><topic>Platelets</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>RECOMBINANT DNA</topic><topic>SACCHARIDES</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Sequencing</topic><topic>SODIUM COMPOUNDS</topic><topic>SODIUM IODIDES</topic><topic>STRUCTURAL CHEMICAL ANALYSIS</topic><topic>SULFUR 35</topic><topic>SULFUR ISOTOPES 550201 -- Biochemistry-- Tracer Techniques</topic><topic>Tandem repeat sequences</topic><topic>TUMOR CELLS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lopez, Jose A.</creatorcontrib><creatorcontrib>Chung, Dominic W.</creatorcontrib><creatorcontrib>Fujikawa, Kazuo</creatorcontrib><creatorcontrib>Hagen, Frederick S.</creatorcontrib><creatorcontrib>Davie, Earl W.</creatorcontrib><creatorcontrib>Roth, Gerald J.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lopez, Jose A.</au><au>Chung, Dominic W.</au><au>Fujikawa, Kazuo</au><au>Hagen, Frederick S.</au><au>Davie, Earl W.</au><au>Roth, Gerald J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The α and β Chains of Human Platelet Glycoprotein Ib are Both Transmembrane Proteins Containing a Leucine-Rich Amino Acid Sequence</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1988-04-01</date><risdate>1988</risdate><volume>85</volume><issue>7</issue><spage>2135</spage><epage>2139</epage><pages>2135-2139</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The primary structure of the β chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence analysis. A λ phage cDNA expression library prepared from human erythroleukemia cells (HEL cells) was screened with a radiolabeled affinity-purified rabbit polyclonal antibody to the β chain of GPIb. Eighteen positive clones were isolated and plaque-purified and the nucleotide sequences of three were determined. The composite sequence spanned 968 nucleotides and included a 5′ untranslated region of 22 nucleotides, an open reading frame of 618 nucleotides encoding a signal peptide of 28 amino acids and a mature protein of 181 amino acids, a stop codon, and a 3′ noncoding region of 307 nucleotides. The 3′ noncoding sequence also contained a polyadenylylation signal (AATAAA) 14 nucleotides upstream from the poly(A) tail of 18 nucleotides. Edman degradation of the intact β chain and of peptides produced by chemical cleavage yielded amino acid sequences spanning 76 residues that were identical to those predicted from the cDNA. The amino-terminal region of the β chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the α chain of GPIb and nine tandem repeats in leucine-rich α 2-glycoprotein. The leucine-rich sequence in the β chain of GPIb is flanked on both sides by amino acid sequences that are similar to those flanking the leucine-rich tandem repeats of the α chain of GPIb and leucine-rich α 2-glycoprotein. The amino-terminal region of the β chain of GPIb is followed by a transmembrane segment of 25 amino acids and an intracellular segment of 34 amino acids at the carboxyl terminus of the protein. The intracellular segment contains an unpaired cysteine and two potential sites for phosphorylation by cAMP-dependent protein kinase.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3353370</pmid><doi>10.1073/pnas.85.7.2135</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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1091-6490
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subjects ALKALI METAL COMPOUNDS
AMINO ACID SEQUENCE
AMINO ACIDS
Analytical, structural and metabolic biochemistry
ANIMAL CELLS
ANTIBODIES
Base Sequence
BASIC BIOLOGICAL SCIENCES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
Biological and medical sciences
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD PLATELETS
BODY FLUIDS
CARBOHYDRATES
CARBOXYLIC ACIDS
CARCINOGENS
CLONING
Complementary DNA
DAYS LIVING RADIOISOTOPES
DISEASES
DNA
DNA - genetics
DNA HYBRIDIZATION
DNA SEQUENCING
DNA-CLONING
ELECTRON CAPTURE RADIOISOTOPES
ELECTROPHORESIS
ESTERS
EVEN-ODD NUCLEI
Fundamental and applied biological sciences. Psychology
GENE REGULATION
GENES
GLUCOPROTEINS
GLYCOPROTEINS
HALIDES
HALOGEN COMPOUNDS
HEMIC DISEASES
Humans
HYBRIDIZATION
IMMUNE SYSTEM DISEASES
INORGANIC PHOSPHORS
INTERMEDIATE MASS NUCLEI
IODIDES
IODINE 125
IODINE COMPOUNDS
IODINE ISOTOPES
ISOTOPES
LEUCINE
Leucine - analysis
LEUKEMIA
LIGHT NUCLEI
MATERIALS
Molecular Sequence Data
MOLECULAR STRUCTURE
NEOPLASMS
NUCLEI
NUCLEIC ACIDS
Nucleotide sequences
Nucleotides
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
PATIENTS
PHORBOL ESTERS
PHOSPHORS
Phosphorylation
Platelet Membrane Glycoproteins - genetics
Platelets
PROTEINS
RADIOISOTOPES
RECOMBINANT DNA
SACCHARIDES
Sequence Homology, Nucleic Acid
Sequencing
SODIUM COMPOUNDS
SODIUM IODIDES
STRUCTURAL CHEMICAL ANALYSIS
SULFUR 35
SULFUR ISOTOPES 550201 -- Biochemistry-- Tracer Techniques
Tandem repeat sequences
TUMOR CELLS
title The α and β Chains of Human Platelet Glycoprotein Ib are Both Transmembrane Proteins Containing a Leucine-Rich Amino Acid Sequence
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