Measurement of total protein in plant samples in the presence of tannins
โ Scribed by David L. Marks; Robert Buchsbaum; Tony Swain
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 657 KB
- Volume
- 147
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
A method for measuring total protein in situ in plant samples has been developed using the determination of amino acids released by acid hydrolysis of dried plant material. Standard proteins and plant samples were hydrolyzed with 3% sulfuric acid at 100ยฐC for 24 h and the amino acids released were measured with ninhydrin. Unhydrolyzed plant extracts were also analyzed for free amino acids with ninhydrin. Total amino acid equivalents (protein plus free amino acids) of a diverse set of plant samples was significantly correlated with total protein as estimated by elemental analysis (N X 6.25). The Lowry method as modified by precipitation of proteins with trichloroacetic acid was found to be unsatisfactory for dried plant samples due to the incomplete extractability of proteins. Although some alkaloids caused increased absorbance with ninhydrin, interference with quantification of protein is likely to be minimal. Tannins interfered with the Lowry and Bradford methods but not the ninhydrin method. o 1985 Academic Press. Inc.
๐ SIMILAR VOLUMES
Measurements of relaxation times in proteins are a valu-simple approach is to measure the efficiency of a sampling pattern applied to several different values of T by the able source of information about molecular motions in biological macromolecules such as proteins (1-3). Relaxation reliability ac