In gel-filtration measurements, prothymosin alpha and its N-terminal fragment thymosin alpha 1m behaved as oligomers (trimers to hexamers).
In plain wordsIn lab tests, prothymosin alpha and its fragment thymosin alpha 1m appeared to form groups of three to six molecules.
- Peptide
- Thymosin alpha-1
- Outcome
- Not applicableOligomeric state in gel filtration
- Study
n: not reported in source
in vitro biophysical measurements- Outcome group
- Receptor activity and mechanism · Pharmacology
Measurements
- relative molecular mass
- 3108
- thymosin alpha 1m
Source sentences
The immunoregulatory polypeptide prothymosin alpha and its biologically active N-terminal fragment thymosin alpha 1m, with relative molecular masses of 12,500 and 3108 respectively, were found to behave as oligomers (trimers to hexamers) in gel-filtration measurements.
In this study, Thymosin alpha-1 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin alpha-1.