Isolation of messenger RNA coding for eggshell protein of the DNA-eliminating nematode Ascaris lumbricoides.

Abstract

Poly(A)-containing RNA from polyploid uterine epithelial cells of Ascaris lumbricoides has been isolated by poly(U)-Sepharose chromatography. The bulk of poly(A)-containing RNA migrates as 18-S RNA in formamide/polyacrylamide gels. In a cell-free wheat germ system, this RNA directs the synthesis of a polypeptide with identical migration behavior in dodecylsulphate/urea/polyacrylamide gels as the polypeptide isolated from the proteinaceous eggshell. The two proteins reveal almost identical peptide patterns in fingerprint analysis. The authentic eggshell protein has been identified as a glycoprotein with a molecular weight of about 10000, as determined by dodecylsulphate/polyacrylamide gel electrophoresis. The apparent discrepancy between mRNA length and the required coding length for the protein is discussed.

• Authors: E Zulauf, C Gut
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 82 Issue 2 Pg. 577-83 (Jan 16 1978) ISSN: 0014-2956 [Print] England
• PMID: 624288 (Publication Type: Journal Article)

Chemical References

• Egg Proteins
• Peptide Fragments
• RNA, Messenger
• Poly A
• DNA

Topics

• Animals
• Ascaris (metabolism)
• DNA (metabolism)
• Egg Proteins (biosynthesis)
• Egg Shell
• Epithelium (metabolism)
• Female
• Molecular Weight
• Peptide Fragments (analysis)
• Poly A
• Protein Biosynthesis
• RNA, Messenger (isolation & purification, metabolism)
• Uterus (metabolism)