Biomedical subjects

P Strózycki

Publications and source records attributed to P Strózycki.

4 recordsLinked to original sources

PubMed1989

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↗

PubMed1988

Isolation and characterization of root nodule proteins from lupin.

A group of root nodule-specific plant proteins (nodulins) has been isolated from yellow lupin (Lupinus luteus) by immunoaffinity chromatography. The cytoplasmic nodule protein extract was initially enriched in nodulins on a column with immobilized IgG fraction. It was then purified by chromatography on Sepharose 4B - bound IgG against uninfected root proteins and finally on Sepharose 4B - bound IgG against Rhizobium lupini proteins. Rocket immunoelectrophoresis showed that the nodulin preparation did not react with antibodies against root or bacterial proteins. SDS gel electrophoresis of lupin nodulins revealed at least 23 polypeptides ranging in Mr, from 7,000 to 70,000, probably representing protein subunits.

Animals↗

PubMed1987

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↗

PubMed1985

Identification and synthesis in vitro of plant-specific proteins in yellow lupin root nodules.

Fifteen to twenty specific polypeptides of Mr ranging from 15 000 to 90 000 were detected using immunochemical techniques in the lupin root nodules and cell-free translation products of the nodule polysomal RNA. These polypeptides were characteristic for symbiotic state of the host plant and represented 9-18% of total nodule proteins. They were absent in uninfected roots and in protein extracts of Rhizobium lupini.

Isoelectric Point↗