Comparative studies on the proteins, carbohydrates, acid phosphatase and ribonuclease in caryopses of two orchardgrass (Dactylis glomerata L.) varieties

Comparative studies were carried out on some biochemical components in caryopses of two varieties of Dactylis glomerata. The determined protein content depended upon the solvent and amounted to 0.22-0.39 g, with sugar amounting to 2.7-3.6 g and pentoses to 0.30-0.67 g per 100 g of caryopses. The level of pentoses, acid phosphatase and ribonuclease activity was about twice higher in the caryopses of the 'Motycka' variety than that in 'Nakielska'. Similar differences in the two varieties were found in the enzyme activity in the seed and chaff of the Dactylis glomerata caryopses

Preliminary studies on ribonucleases from Poa pratensis seeds

Ribonuclease was extracted from Poa pratensis seeds with 0.1 M acetate buffer, pH 5.1, and then precipitated with alcohol. The enzyme was separated into 5 fractions (I-V) after chromatography on DEAE-cellulose at pH 5.1. The enzymes were stable at 50°C, at pH 7.1. The activity of ribonucleases I, II, III and V were optimal at pH 7.1-7.3, and that of ribonuclease IV at pH 8.1. Ali enzymes were inhibited by Ca2+ and EDTA. Mg2+ inhibited the activity of ribonucleases II, III, IV, and had no influence on that of ribonucleases I and V. Ribonucleases IV and V showed only one activity band in disc electrophoresis, whereas ribonucleases, I, II and III were found to be heterogenous

Acid phosphatase from stored Poa pratensis caryopses and its ability for binding to lectins

The effect of the storage period of Poa pratensis caryopses on acid phosphatase activity and on the ability of this enzyme to interact with lectins has been studied. It has been shown that after ten years of caryopses storage, the activity of acid phosphatase decreased about 50 per cent, while the content of proteins and carbohydrates did not change. The decrease of enzyme activity during the long period of storage was found only in seeds, but not in chaffs. Acid phosphatase was isolated from caryopses stored one, two, three, five and ten years. The enzyme showed the ability to bind to immoblized as well as to free conA during the whole period of storage, hut did not react with Wheat Germen Agglutinin (WGA). The activation of acid phosphatase by binding to conA decreased with the length of storage period