Quantitative Differences between N-terminal Methionyl Nascent Globin Chains of Human and Rabbit Reticulocytes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1973-11

AUTHORS

HARUO SUZUKI, HARVEY A. ITANO

ABSTRACT

INCORPORATION of methionine as N-terminal residue initiates biosynthesis of a globin chain in rabbit reticulocytes1–7. After initiation, elongation of the chain proceeds with successive additions of amino acid residues; therefore a population of actively synthesising polysomes contains nascent peptide chains of all stages of elongation8. The initial methionine residue is removed before completion of the chain; consequently methionine is the N-terminal residue of short nascent chains, and valine, the second amino acid incorporated, is the N-terminal residue of long nascent chains. When these chains are digested with trypsin, long nascent chains yield the same N-terminal tryptic peptides as haemoglobin, αT1 of α chain and βT1 of β chain, which have N-terminal valine and are composed of seven and eight amino acid residues, respectively9, 10. The N-terminal tryptic peptides of short nascent chains are longer by one residue, namely the N-terminal methionine. Thus all but very short nascent chains contain either the methionyl or the valyl N-terminal tryptic peptide, and the ratio of yields of these peptides from a tryptic digest is a measure of the relative numbers of the two types of nascent chains in a polysomal preparation. More... »

PAGES

107

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/newbio246107a0

DOI

http://dx.doi.org/10.1038/newbio246107a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022137794

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4518934


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