Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2008 Aug 14;189(1-4):203–206. doi: 10.1159/000151376

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2008 by S. Karger AG, Basel

PMC Copyright notice

Fig. 2. — Comparative hydrolysis of wild-type and mutated amelogenins in solution or on HAP. Hydrolyzed wild-type amelogenin (rh174) and 2 mutants (P156T and P164T) were analyzed by SDS-PAGE and the protein bands were quantified using the NIH Image software. The digestion rates of the proteins, either in solution (a) or bound on HAP (b), were compared by the ratio of substrate at time t to substrate at time zero (S_t/S₀). Both in solution and on HAP, the P164T amelogenin mutant had a much higher S_t/S₀ ratio than the wild-type and P156T amelogenins.

Fig. 2. — Comparative hydrolysis of wild-type and mutated amelogenins in solution or on HAP. Hydrolyzed wild-type amelogenin (rh174) and 2 mutants (P156T and P164T) were analyzed by SDS-PAGE and the protein bands were quantified using the NIH Image software. The digestion rates of the proteins, either in solution (a) or bound on HAP (b), were compared by the ratio of substrate at time t to substrate at time zero (S_t/S₀). Both in solution and on HAP, the P164T amelogenin mutant had a much higher S_t/S₀ ratio than the wild-type and P156T amelogenins.