Two uncommon phospholipase D isoenzymes from poppy seedlings (Papaver somniferum L.) (Record no. 47451)
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| 000 -LEADER | |
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| fixed length control field | 02122nam a2200265Ia 4500 |
| 003 - CONTROL NUMBER IDENTIFIER | |
| control field | MX-MdCICY |
| 005 - DATE AND TIME OF LATEST TRANSACTION | |
| control field | 20250625153919.0 |
| 040 ## - CATALOGING SOURCE | |
| Transcribing agency | CICY |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) | |
| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) | B-13250 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION | |
| fixed length control field | 250602s9999 xx |||||s2 |||| ||und|d |
| 245 10 - TITLE STATEMENT | |
| Title | Two uncommon phospholipase D isoenzymes from poppy seedlings (Papaver somniferum L.) |
| 490 0# - SERIES STATEMENT | |
| Volume/sequential designation | Biochimica et Biophysica Acta, 1631(2), p.153-159, 2003 |
| 520 3# - SUMMARY, ETC. | |
| Summary, etc. | Phospholipase D (PLD)has been detected in seedlings of Papaver somniferum L. cv. Lazu´ r (Papaveraceae). Purification of the enzyme revealed the existence of two forms of PLD (named as PLD-A and PLD-B). The two enzymes strongly differ in their catalytic properties. The pH optima were found at pH 8.0 for PLD-A and at pH 5.5 for PLD-B. While both enzymes show hydrolytic activity toward phosphatidylcholine (PC)and phosphatidyl-p-nitrophenol (PpNP), PLD-B only was able to catalyze the exchange of choline in PC by glycerol. Both enzymes were activated by Ca2 + ions with an optimum concentration of 10 mM. In contrast to PLDs from other plants, LD-B was still more activated by Zn2 + ions with an optimum concentration of 5 mM. The apparent molecular masses of PLD-A and PLD-B, derived from sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE), were estimated to be 116.4 and 114.1 kDa. N-terminal protein sequencing indicated N-terminal blockage in both cases. The isoelectric points were found to be 8.7 for PLD-A and 6.7 for PLD-B. Both enzymes were shown to be N-linked glycoproteins. This paper is the first report on PLD in poppy and indicates some important differences of the two enzyme forms to other PLDs known so far. |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM | |
| Topical term or geographic name entry element | PHOSPHOLIPASE D |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM | |
| Topical term or geographic name entry element | PAPAVER SOMNIFERUM |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM | |
| Topical term or geographic name entry element | PURIFICATION |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM | |
| Topical term or geographic name entry element | ZN-ACTIVATION |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM | |
| Topical term or geographic name entry element | TRANSPHOSPHATIDYLATION |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Oblozinsky, M. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Schoeps, R. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Ulbrich-Hofmann, R. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Bezakova, L. |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Uniform Resource Identifier | <a href="https://drive.google.com/file/d/1Xmvhn1XCXbNqiSWKDEylY0DIrqQh8SGu/view?usp=drivesdk">https://drive.google.com/file/d/1Xmvhn1XCXbNqiSWKDEylY0DIrqQh8SGu/view?usp=drivesdk</a> |
| Public note | Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
| Source of classification or shelving scheme | Clasificación local |
| Koha item type | Documentos solicitados |
| Lost status | Source of classification or shelving scheme | Damaged status | Not for loan | Collection | Home library | Current library | Shelving location | Date acquired | Total checkouts | Full call number | Date last seen | Price effective from | Koha item type |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Clasificación local | Ref1 | CICY | CICY | Documento préstamo interbibliotecario | 25.06.2025 | B-13250 | 25.06.2025 | 25.06.2025 | Documentos solicitados |
