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Typus
BauernOpfer
Bearbeiter
SleepyHollow02
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Untersuchte Arbeit:
Seite: 9, Zeilen: 1 ff. (entire page)
Quelle: Wiedenmann 2000
Seite(n): 14092, Zeilen: r.col.: 8 ff.
Tim 009a diss.png

Fig. 3. Pigments of A. sulcata var. rufescens. (A) Localization of GFPs in the upper side, orange fluorescent protein in the underside, and reddish protein in the tips of tentacles under daylight (scale bar: 1 cm) and UV (366 nm) (B). (C) Kryo-section (20 mm) of a tentacle fixed in seawatery4% paraformaldehyde irradiated with UV (365 nm) shows the ectodermal localization of the fluorescent proteins. The orange fluorescent protein located in the underside of the tentacle shows a yellow-shifted emission. This shift most likely is induced by the fixation. The red fluorescence of the entoderm is produced by chlorophyll of zooxanthellae (scale bar: 0.5 mm). (Wiedenmann et al., 2000).

Spectral properties.

The spectral properties are summarized in table 1 (appendixes) (Wiedenmann et al., 2000). The green fluorescence of partially purified protein solutions is characterized by an excitation spectrum with two maxima at 480 nm and 511 nm and a shoulder around 400 nm. A region of high excitation is found in the UV spectrum.

The emission spectrum shows two maxima at 499 nm and 522 nm. The ratio between the emission maxima varies in dependence of the excitation wavelength. This points to the existence of two different forms of GFP in the tissue with excitation/emission maxima at 480 nm/499 nm and 511 nm/522 nm.

The orange fluorescence distinguishes itself by three excitation maxima at 278 nm, 337 nm, and 574 nm and a single emission peak at 595 nm.

In the visible region the maximum of absorption of the nonfluorescent red protein is at 562 nm. According to the nomenclature introduced by Matz et al. (1999) the fluorescent proteins from A. sulcata var. rufescens were named asFP499, asFP522, and asFP595. The nonfluorescent red protein from A. sulcata var. rufescens was named asCP562. In this context, CP stands for colored protein and the number identifies the major absorption maximum.

Spectral properties. The spectral properties are summarized in Table 1. The green fluorescence of partially purified protein solutions is characterized by an excitation spectrum with two maxima at 480 nm and 511 nm and a shoulder around 400 nm. A region of high excitation is found in the UV spectrum. The emission spectrum shows two maxima at 499 nm and 522 nm (Fig. 2A). The ratio between the emission maxima varies in dependence of the excitation wavelength. Such a variance also is found in samples derived from different specimens (data not shown). This points to the existence of two different forms of GFP in the tissue with excitation/emission maxima at 480 nm/499 nm and 511 nm/522 nm. The orange fluorescence distinguishes itself by three excitation maxima at 278 nm, 337 nm, and 574 nm and a single emission peak at 595 nm (Fig. 2A). In the visible region the maximum of absorption of the nonfluorescent red protein is at 562 nm (Fig. 2C).

According to the nomenclature introduced by Matz et al. (22) the fluorescent proteins from A. sulcata var. rufescens were named asFP499, asFP522, and asFP595. The nonfluorescent red protein from A. sulcata var. rufescens was named asCP562. In this context, CP stands for colored protein and the number identifies the major absorption maximum.

Tim 009a source.png

Fig. 1. Pigments of A. sulcata var. rufescens. (A) Localization of GFPs in the upper side, orange fluorescent protein in the underside, and reddish protein in the tips of tentacles under daylight (scale bar: 1 cm) and UV (366 nm) (B). (C) Kryo-section (20 mm) of a tentacle fixed in seawatery4% paraformaldehyde irradiated with UV (365 nm) shows the ectodermal localization of the fluorescent proteins. The orange fluorescent protein located in the underside of the tentacle shows a yellow-shifted emission. This shift most likely is induced by the fixation. The red fluorescence of the entoderm is produced by chlorophyll of zooxanthellae (scale bar: 0.5 mm).

Anmerkungen

Source is mentioned twice: once to reference the image and its caption and once for table 1. It does not become clear to the reader, however, that the entire page is taken from the source.

Sichter
(SleepyHollow02), Hindemith

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