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. 1985 Jul;82(13):4486–4489. doi: 10.1073/pnas.82.13.4486

Amino-terminal amino acid sequence of murine colony-stimulating factor 1.

C M Ben-Avram, J E Shively, R K Shadduck, A Waheed, T Rajavashisth, A J Lusis
PMCID: PMC391126  PMID: 3925458

Abstract

We report the amino acid composition, the NH2-terminal sequence, and the tryptic map by HPLC for murine L-cell colony-stimulating factor 1 (CSF-1). CSF-1 purified by affinity chromatography was S-carboxymethylated under denaturing conditions and subjected to sequence microanalysis. CSF-1 contains four or five cysteine residues per subunit and approximately 30-40% carbohydrate by weight. Three contiguous cysteine residues were located in the NH2-terminal sequence. An additional two cysteine residues were located on the tryptic map. Previous studies as well as immunoblotting studies reported here suggest that sulfhydryl bridging plays a major role in maintaining the conformation of the protein. Carbohydrate was located on two tryptic fragments. The findings of a single NH2-terminal sequence in high yield and a relatively simple tryptic map (15 major peptides) suggest that CSF-1 contains two identical subunits. The NH2-terminal sequence of CSF-1 has only limited homology to insulin or insulin-like hormones but no homology with granulocyte/macrophage-CSF or interleukin 3.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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