ArticleProtein science : a publication of the Protein Society2002
Covalent cross-linking of proteins without chemical reagents.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 38 citations in OpenAlex.
- Intra- vs Intermolecular Cross-Links in Poly(methyl methacrylate) Networks Containing Enamine Bonds.Macromolecules · 2022Article
- Correlations between Photodegradation of Bisretinoid Constituents of Retina and Dicarbonyl Adduct Deposition.The Journal of biological chemistry · 2015Article
- Kinetics and mechanisms of deamidation and covalent amide-linked adduct formation in amorphous lyophiles of a model asparagine-containing Peptide.Pharmaceutical research · 2012Article
- Nanodiamonds as Carriers for Address Delivery of Biologically Active Substances.Nanoscale research letters · 2010Article
- "Zero-length" cross-linking in solid state as an approach for analysis of protein-protein interactions.Protein science : a publication of the Protein Society · 2006Article
- Activity of glucose oxidase functionalized onto magnetic nanoparticles.Biomagnetic research and technology · 2005Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A facile method for the formation of zero-length covalent cross-links between protein molecules in the lyophilized state without the use of chemical reagents has been developed. The cross-linking process is performed by simply sealing lyophilized protein under vacuum in a glass vessel and heating at 85 degrees C for 24 h. Under these conditions, approximately one-third of the total protein present becomes cross-linked, and dimer is the major product. Chemical and mass spectroscopic evidence obtained shows that zero-length cross-links are formed as a result of the condensation of interacting ammonium and carboxylate groups to form amide bonds between adjacent molecules. For the protein examined in the most detail, RNase A, the cross-linked dimer has only one amide cross-link and retains the enzymatic activity of the monomer. The in vacuo cross-linking procedure appears to be general in its applicability because five different proteins tested gave substantial cross-linking, and co-lyophilization of lysozyme and RNase A also gave a heterogeneous covalently cross-linked dimer.
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