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B Golińska

Publications and source records attributed to B Golińska.

4 recordsLinked to original sources

Accumulation of mycotoxins in forage of winter pasture during prolonged utilisation of sward.

The concentration of mycotoxins in sward depending on time of pre-utilisation in summer and date of harvest in winter was analysed during the 2000-2002 vegetation seasons. Additionally, the yield of pasture sward was estimated. Higher concentrations of ochratoxin A--respectively: 0.55 and 050 ng/g DM--were found in the pasture sward harvested in December and January when compared to the sward collected in November (0.36 ng/g DM). The average concentration of zearalenone varied from 2.74 ng/g DM in December, to 6.00 ng/g DM in November and 9.77 ng/g DM in January. The highest concentration of ochratoxin A was 1.82 ng/g DM and zearalenone 47.89 ng/g DM. The highest number of samples in which ochratoxin A exceeded the level of 0.3 ng/g DM was noted in sward harvested in January (61.1%), while in the case of zearalenone, the number of samples containing this mycotoxin at a level exceeding 3.0 ng/g DM varied from 55.6% in December to 66.7% in November and January. It seems that the percentage of ochratoxin A positive samples and the toxin concentration level in the sward of winter pastures increased during the time of sward regrowth.

Animal Feed↗

Coordinated synthesis of leghemoglobin and root protein R18 in yellow lupin.

Uninfected roots of yellow lupin contain an abundant 18 kDa protein (referred to as R18), absent in the mature nodules. Some properties of this polypeptide are apparently similar to those of lupin leghemoglobins. However, the lack of any immuno crossreaction between R18 and leghemoglobin and differences in N-terminal amino acid sequences indicate that these proteins are coded by different genes. The decrease in the content of R18 protein in developing nodule is associated with the increased synthesis of leghemoglobin. This implies coordination of both events.

Amino Acid Sequence↗

Lupin leghemoglobins during root nodule development.

Two yellow lupin leghemoglobins, Lb I and Lb II, were purified to homogeneity using the HPLC technique for final separation. Lb I and Lb II were identified by the N-terminal sequences and their reaction with antibodies against electrophoretically pure leghemoglobin. The third Lb species was detected by the combined method of isoelectrofocusing and PAGE of Lb I. It seems that Lb III represents a posttranslational modification of Lb I. Developmental changes in Lb multiple forms were examined using the Western blotting method. The content of leghemoglobin, first detectable approximately 3 weeks after infection, increased up to 6-7 weeks, and then it remained at the same level until 8-9 weeks after the infection. At the early stages of nodule formation Lb I prevailed over Lb II, while later Lb II became the predominant form. This suggests physiological role of particular forms and precise regulation of the expression of Lb genes.

Amino Acid Sequence↗