-
Inhibitorji cisteinskih proteinaz kot potencialne obrambne molekule za zaščito rastlin : doktorska disertacija = Cysteine proteinase inhibitors as potential plant defense molecules : dissertation thesisRogelj, BorisOne of the mechanisms of plant defense against pests involves proteinase inhibitors (PI), which interfere with pestćs digestive proteolytic activity. With transgenic technology, PI genes from other ... species can be introduced intoplants to improve their defensive capabilities. This procedure involves screening for and isolation of new PIs, in vitro and in vivo bioassays, introduction of the chosen gene into the plant and optimisation of expression of the recombinant PI in the plant. Our screening of various plant and fungal material for cysteine prateirmse inhibitors showed that protein extracts from the greater celandine, Chelidonium majus, and a basidiomycete mushroom, Clitocybe nebularis, strongly inhibit papain. Two novel inhibitors of cysteineproteinases were isolated, chelidocystatin (from C majus) and clitocypin (from C. nebularis). Chelidocystatin showed a mass of 10 kDa and a pI of 9.3. It is a strong inhibitor of cathepsin L (Ki = 0.056 nM), papain (Ki= 0.11 nM) and cathepsin H (Ki = 7.5 nM). Comparison of the complete amino acid sequence showed that it is a member of phytocistatin family within the superfamily of cystatins. Clitocypin has a larger mass of 34 kDa which, under strong denaturating conditions only, yielded a single band at 17 kDa, suggesting a homodimer composition with no disulphide bonds. The inhibitor hasan isoelectric point of 4.4. It was found to be a tight-binding inhibitor of papain (Ki = 0.58 nM), cathepsin L (Ki = 0.83 nM ) and cathepsin B (Ki = 480 nM), but a very poor inhibitor of cathepsin H, and has no activity towardstrypsin or cathepsin D. The complete amino acid sequence of clitocypin bears no similarity to any other cysteine proteinase inhibitor (CPI) nor to any other protein, suggesting a completely novel type of CPI. (Abstract truncated at 2000 characters.)Vrsta gradiva - disertacijaZaložništvo in izdelava - Ljubljana : [B.Rogelj], 1999Jezik - slovenskiCOBISS.SI-ID - 2057748
Avtor
Rogelj, Boris
Drugi avtorji
Kregar, Igor, 1937-2017 |
Štrukelj, Borut
Teme
Cysteine proteinase inhibitors |
Isolation and purification |
Cysteine proteinase inhibitors |
Chemistry |
Plant physiology |
Inhibitorji cisteinske proteinaze |
Izolacija in čiščenje |
Inhibitorji cisteinske proteinaze |
Kemija |
Rastlinska fiziologija |
biokemija |
molekularna biologija
![loading ... loading ...](themes/default/img/ajax-loading.gif)
Knjižnica/institucija |
Kraj | Akronim | Za izposojo | Druga zaloga |
---|---|---|---|---|
MF, Centralna medicinska knjižnica, Ljubljana | Ljubljana | CMK |
na dom 2 izv.
|
|
Narodna in univerzitetna knjižnica, Ljubljana | Ljubljana | NUK |
v čitalnico 1 izv.
|
|
Univerzitetna knjižnica Maribor | Maribor | UKM |
v čitalnico 1 izv.
|
ni za izposojo 1 izv.
|
![loading ... loading ...](themes/default/img/ajax-loading.gif)
![loading ... loading ...](themes/default/img/ajax-loading.gif)
![loading ... loading ...](themes/default/img/ajax-loading.gif)
Vnos na polico
Trajna povezava
- URL:
Faktor vpliva
Dostop do baze podatkov JCR je dovoljen samo uporabnikom iz Slovenije. Vaš trenutni IP-naslov ni na seznamu dovoljenih za dostop, zato je potrebna avtentikacija z ustreznim računom AAI.
Leto | Faktor vpliva | Izdaja | Kategorija | Razvrstitev | ||||
---|---|---|---|---|---|---|---|---|
JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
Baze podatkov, v katerih je revija indeksirana
Ime baze podatkov | Področje | Leto |
---|
Povezave do osebnih bibliografij avtorjev | Povezave do podatkov o raziskovalcih v sistemu SICRIS |
---|---|
Rogelj, Boris | 15813 |
Kregar, Igor, 1937-2017 | 01084 |
Štrukelj, Borut | 07849 |
Izberite prevzemno mesto:
Prevzem gradiva po pošti
Obvestilo
Gesla v Splošnem geslovniku COBISS
Izbira mesta prevzema
Mesto prevzema | Status gradiva | Rezervacija |
---|
Prosimo, počakajte trenutek.