COMPARISON OF TRYPSIN X-IRRADIATED IN SOLUTION AND IN AGAR GELS

Journal Article · Thu Sep 01 04:00:00 EDT 1960 · Journal of Physical Chemistry (U.S.)

DOI:https://doi.org/10.1021/j100838a023· OSTI ID:4135134

Augenstine, E S; Augenstine, L G; Lippincott, E R

A method was developed to measure the enzymatic activity of trypsin recovered from agar gels. From unirradiated gels this activity was always less than that from a corresponding solution containing no agar. The amount of trypsin inactivated in gels by a given dose of radiation was much less than that in trypsin solutions where there was no agar. This was contrary to expectations based on previous studies of gels containing dyes. This inhibition of inactivation in agar is presumed to result from an interaction between agar and trypsin. For example, a complex may form such that susceptible sites of the trypsin are shielded from reaction with radiationproduced radicals. Alternatively, the micellular structure of agar may hinder the trypsin from unfolding once it reacts with a radical. (auth)

• Research Organization: Univ. of Maryland, College Park; and Brookhaven National Lab., Upton, N.Y.
• Sponsoring Organization: USDOE
• NSA Number: NSA-14-025518
• OSTI ID: 4135134
• Journal Information: Journal of Physical Chemistry (U.S.), Journal Name: Journal of Physical Chemistry (U.S.) Vol. Vol: 64; ISSN JPCHA
• Country of Publication: Country unknown/Code not available
• Language: English

Related Subjects

ALGAE
CHEMISTRY
COLLOIDS
ENZYMES
FREE RADICALS
IRRADIATION
MEASURED VALUES
RADIATION EFFECTS
RECOVERY
TRYPSIN
X RADIATION