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Cited by 270

The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.

Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated.

Open access
Brown, J L, Roberts, W K·1976·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)33793-6
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Abstract

Analysis of soluble Ehrlich ascites proteins by the Sanger procedure revealed methionine, alanine, valine, and glycine as the major NH2-terminal amino acids. The average monomer weights of these proteins calculated from the yields of NH2-terminal amino acids was 144,000. In contrast, the average monomer weight of Ehrlich ascites soluble proteins calculated from the data obtained after electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate was 32,500. The explanation for the disparity in the estimates of average monomer weight obtained by the procedures appears to be that extensive blocking of alpha-NH2 groups by acetate occurs in these proteins, i.e. of the acetate present in the acidic peptides isolated from proteolytic digests of ascites proteins, 23.2 nmol/mg of protein appears to originate from N-acetyl amino acids. These results suggest that approximately 80% of the soluble proteins from Ehrlich ascites cells contain acetate at their NH2-terminal residues. The extensive N-acetylation of proteins does not appear to be limited to Ehrlich ascites cells and may be characteristic of eukaryotic proteins.

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Metadata

Authors
Brown, J. L., & Roberts, W. K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1976-02
Volume
251
Issue
4
Pages
1009-1014
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(17)33793-6
OpenAlex
W1526449859
Cited by
270
References
22
FWCI
4.19
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated. https://app.cochat.ai/papers/10.1016/s0021-9258(17)33793-6
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Brown, J. L., & Roberts, W. K. (1976). Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)33793-6

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.