Abstract
1. 1. Fructose-bisphosphate aldolase from Helix pomatia is a tetramer of 40,000 mol. wt. sub-units like mammalian aldolases. 2. 2. The snail enzyme differs slightly in amino acid composition from mammalian aldolases and has glycine as its amino terminus rather than proline. 3. 3. Spectroscopic measurements (u.v., fluorescence, ORD, CD) show small yet definite differences in secondary structure between the snail and mammalian aldolases but indicate thaT no major structural changes have occurred during evolution.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
