Controlled cleavage of KLH1 and KLH2 by the V8 protease from Staphylococcus aureus reassociation, electrophoretic and transmission electron microscopy study of peptide fragments.
Open Access
- 15 May 1999
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 262 (1) , 166-175
- https://doi.org/10.1046/j.1432-1327.1999.00364.x
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Mass Determination, Subunit Organization and Control of Oligomerization States of Keyhole Limpet Hemocyanin (KLH)European Journal of Biochemistry, 1997
- Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitutionJournal of Molecular Biology, 1997
- Keyhole limpet hemocyanin (KLH), I: Reassociation from Immucothel® followed by separation of KLH1 and KLH2Micron, 1997
- Keyhole limpet hemocyanin (KLH), II: Characteristic reassociation properties of purified KLH1 and KLH2Micron, 1997
- HemocyaninsAdvances in Protein Chemistry, 1995
- Keyhole limpet haemocyanin (KLH): Purification of intact KLH1 through selective dissociation of KLH2Micron, 1995
- Two-dimensional crystallization, transmission electron microscopy and image processing of keyhole Limpet Haemocyanin (KLH)Micron and Microscopica Acta, 1992
- The role of two distinct subunit types in the architecture of keyhole limpet hemocyanin (KLH)The Science of Nature, 1991
- Structure of Helix pomatia Oxy-beta-hemocyanin and Deoxy-beta-hemocyanin Tubular PolymersEuropean Journal of Biochemistry, 1979
- Tubular Polymers Derived from Helix pomatiaβ‐HemocyaninEuropean Journal of Biochemistry, 1975