NH 2 -terminal residues of Neurospora crassa proteins
- PMID: 5095291
- PMCID: PMC247009
- DOI: 10.1128/jb.107.3.840-845.1971
NH 2 -terminal residues of Neurospora crassa proteins
Abstract
The NH(2)-terminal amino acid composition of the soluble and ribosomal proteins from Neurospora crassa mycelia and conidia was determined by the dinitrophenyl method. A nonrandom distribution of NH(2)-terminal amino acids was observed in the complex protein mixtures. Glycine, alanine, and serine accounted for 75% of the NH(2)-terminal amino acids, and glycine appeared most frequently in mature proteins of mycelia. The appearance of phenylalanine as one of the major NH(2)-termini in crude conidial fraction suggests that the composition of proteins may vary in different developmental stages.
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