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1.题目Germination and viability of the pollen of Crocus sativus L
  作者Giuseppe Chichiricco; Maria Grilli Caiola
  摘要Abstract  Viability and germinability tests were carried out on the pollen of Crocus sativus L., a sterile triploid commonly known as saffron. Pollen taken from dehiscent anthers was examined by means of vital staining and cytochemical techniques in order to detect its viability; germination in vitro was evaluated. From the results obtained it is evident that saffron pollen is viable at a high percentage (65%) but germinates at a very low percentage. Moreover in vitro germination is very slow, and is accompained by numerous morphological anomalies. The low germination of the pollen is due to the triploidy of C. sativus.

链接：http://www.informaworld.com/smpp/content~db=jour~content=a914807526

2.题目Isolation of a new fungi and wound-induced chitinase class in corms of Crocus sativus.

来源<a href="" 'jour', 'Plant Physiol Biochem.');" >Plant Physiol Biochem. 2009 May;47(5):426-34
摘要In plants, various chitinases have been identified and categorized into several groups based on the analysis of their sequences and domains. We have isolated SafchiA, a novel class of chitinase from saffron (Crocus sativus L.). The cDNA encoding SafchiA is mainly expressed in roots and corms, and its expression is induced by elicitor treatment, methyl jasmonate, wounding, and by the fungi Fusarium oxysporum, Beauveria and Phoma sp., suggesting a defence role of the protein. Furthermore, in vitro assays with the recombinant native protein showed chitinolytic, and antifungal activity. The deduced protein shares high similarity with chitinases belonging to family 19 of glycosyl-hydrolases, although some changes in the enzyme active site are present. To explore the properties of SafchiA we have expressed recombinant SafchiA in Escherichia coli and generated four different mutants affected in residues involved in the catalytic activity. One glutamic acid essential for family 19 chitinases activity is not present in C. sativus chitinase suggesting that only one acidic residue is necessary for the enzyme activity, in a similar manner as family 18 glycosyl-hydrolases.
链接：http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=pubmed&dopt=abstract&list_uids=19246207