Human fibronectin is synthesized as a pre-propolypeptide

Fibronectins (FNs) are extracellular glycoproteins consisting of dimers or multimers of similar but not identical subunits. The subunit differences result from variations in internal primary sequence due to alternative splicing in at least 2 regions of the pre-mRNA. The complete amino acid sequence...

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Guardado en:
Detalles Bibliográficos
Publicado: 1986
Materias:
(Human)
cDNA
Fibronectin
Pro-peptide
Signal peptide
complementary dna
fibronectin
protein precursor
radioisotope
signal peptide
amino acid sequence
cell culture
genetic engineering
heredity
human
human cell
in vitro study
priority journal
protein processing
protein structure
protein synthesis
Amino Acid Sequence
DNA
Fibronectins
Human
Peptides
Protein Precursors
RNA, Messenger
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v207_n1_p145_Gutman
http://hdl.handle.net/20.500.12110/paper_00145793_v207_n1_p145_Gutman
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_00145793_v207_n1_p145_Gutman
record_format dspace
spelling paper:paper_00145793_v207_n1_p145_Gutman2023-06-08T14:37:32Z Human fibronectin is synthesized as a pre-propolypeptide (Human) cDNA Fibronectin Pro-peptide Signal peptide complementary dna fibronectin protein precursor radioisotope signal peptide amino acid sequence cell culture genetic engineering heredity human human cell in vitro study priority journal protein processing protein structure protein synthesis Amino Acid Sequence DNA Fibronectins Human Peptides Protein Precursors RNA, Messenger Fibronectins (FNs) are extracellular glycoproteins consisting of dimers or multimers of similar but not identical subunits. The subunit differences result from variations in internal primary sequence due to alternative splicing in at least 2 regions of the pre-mRNA. The complete amino acid sequence of mature human cellular FN has been reported recently from cDNA cloning and sequencing. The same approach has now enabled us to deduce, for the first time, that FN has a 26 amino acid signal peptide and that it undergoes proteolytic processing at its N-terminus to eliminate a 5 amino acid pro-sequence (Ser-Lys-Ser-Lys-Arg). The signal sequence matches the consensus format, while this pro-sequence is a distinctive, very hydrophilic and basic peptide. © 1986. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v207_n1_p145_Gutman http://hdl.handle.net/20.500.12110/paper_00145793_v207_n1_p145_Gutman
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic (Human)
cDNA
Fibronectin
Pro-peptide
Signal peptide
complementary dna
fibronectin
protein precursor
radioisotope
signal peptide
amino acid sequence
cell culture
genetic engineering
heredity
human
human cell
in vitro study
priority journal
protein processing
protein structure
protein synthesis
Amino Acid Sequence
DNA
Fibronectins
Human
Peptides
Protein Precursors
RNA, Messenger
spellingShingle (Human)
cDNA
Fibronectin
Pro-peptide
Signal peptide
complementary dna
fibronectin
protein precursor
radioisotope
signal peptide
amino acid sequence
cell culture
genetic engineering
heredity
human
human cell
in vitro study
priority journal
protein processing
protein structure
protein synthesis
Amino Acid Sequence
DNA
Fibronectins
Human
Peptides
Protein Precursors
RNA, Messenger
Human fibronectin is synthesized as a pre-propolypeptide
topic_facet (Human)
cDNA
Fibronectin
Pro-peptide
Signal peptide
complementary dna
fibronectin
protein precursor
radioisotope
signal peptide
amino acid sequence
cell culture
genetic engineering
heredity
human
human cell
in vitro study
priority journal
protein processing
protein structure
protein synthesis
Amino Acid Sequence
DNA
Fibronectins
Human
Peptides
Protein Precursors
RNA, Messenger
description Fibronectins (FNs) are extracellular glycoproteins consisting of dimers or multimers of similar but not identical subunits. The subunit differences result from variations in internal primary sequence due to alternative splicing in at least 2 regions of the pre-mRNA. The complete amino acid sequence of mature human cellular FN has been reported recently from cDNA cloning and sequencing. The same approach has now enabled us to deduce, for the first time, that FN has a 26 amino acid signal peptide and that it undergoes proteolytic processing at its N-terminus to eliminate a 5 amino acid pro-sequence (Ser-Lys-Ser-Lys-Arg). The signal sequence matches the consensus format, while this pro-sequence is a distinctive, very hydrophilic and basic peptide. © 1986.
title Human fibronectin is synthesized as a pre-propolypeptide
title_short Human fibronectin is synthesized as a pre-propolypeptide
title_full Human fibronectin is synthesized as a pre-propolypeptide
title_fullStr Human fibronectin is synthesized as a pre-propolypeptide
title_full_unstemmed Human fibronectin is synthesized as a pre-propolypeptide
title_sort human fibronectin is synthesized as a pre-propolypeptide
publishDate 1986
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v207_n1_p145_Gutman
http://hdl.handle.net/20.500.12110/paper_00145793_v207_n1_p145_Gutman
_version_ 1768546659017424896

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