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Observationobservedoriginal resultmeasured

Claim · model-written summary

The Sphaerocarpos pigment had difference spectrum maxima at 655 and 720 nm.

Taxon
SphaerocarposSphaerocarpose2
Outcome
difference spectrum maximae2
Value
655 and 720 nme2

Verbatim

t0

“Liverwort Sphaerocarpos”

✓ located verbatim in the source · title, characters 55–78
e2

“Corresponding difference spectrum maxima for the Sphaerocarpos pigment were at 655 and 720 nm”

✓ located verbatim in the source · abstract, characters 202–295

Title

Isolation of Phytochrome from the Alga Mesotaenium and Liverwort Sphaerocarpos

A. O. Taylor; Bruce A. Bonner PLANT PHYSIOLOGY 1967. doi:10.1104/pp.42.6.762

Other claims from this paper (4)
Observationobservedoriginal resultmeasured

Claim · model-written summary

(GlcNAc)3 induced a UV-difference spectrum of rye seed chitinase-a with maxima at 284 and 293 nm.

Treatment
(GlcNAc)3e3
Outcome
UV-difference spectrume3
Value
284 and 293 nme3

Verbatim

t0

“Rye Seed Chitinase-a”

✓ located verbatim in the source · title, characters 87–107
e3

“This oxidation was prevented by (GlcNAc)3, which induced a high UV-difference spectrum with maxima at 284 and 293 nm”

✓ located verbatim in the source · abstract, characters 664–780

Title

Involvements of Trp23 in the Chitin-binding and of Trp131 in the Chitinase Activity of Rye Seed Chitinase-a

Takeshi Yamagami; Gunki Funatsu Bioscience Biotechnology and Biochemistry 1997. doi:10.1271/bbb.61.1819

Other claims from this paper (12)
Observationobservedoriginal resultmeasured

Claim · model-written summary

(GlcNAc)4 induced a UV-difference spectrum with maxima at 284 nm and 293 nm, similar to that of RSC-c.

Treatment
(GlcNAc)4e6
Outcome
UV-difference spectrume6
Value
284 nm and 293 nme6
Comparator
RSC-ce6

Verbatim

t0

“Rye Seed Chitinase-a”

✓ located verbatim in the source · title, characters 87–107
e6

“The NBS oxidation of the isolated Cat domain at pH 5.9 was protected by (GlcNAc)4, which induced a UV-difference spectrum with maxima at 284 nm and 293 nm as well as a small trough around 300 nm, similar to that observed in RSC-c”

✓ located verbatim in the source · abstract, characters 1048–1277

Title

Involvements of Trp23 in the Chitin-binding and of Trp131 in the Chitinase Activity of Rye Seed Chitinase-a

Takeshi Yamagami; Gunki Funatsu Bioscience Biotechnology and Biochemistry 1997. doi:10.1271/bbb.61.1819

Other claims from this paper (12)
Observationobservedoriginal resultmeasured

Claim · model-written summary

Oat phytochrome synthesized in tobacco resembled the oat protein in spectrum, dark reversion and dimer size.

Gene
Oat phytochromee0
Outcome
photoreversible difference spectrum maximae0
Value
665 and 730 nanometerse0
Comparator
etiolated oatse0

Verbatim

e0

“Oat phytochrome synthesized in tobacco is indistinguishable from that present in etiolated oats, having photoreversible difference spectrum maxima at 665 and 730 nanometers, exhibiting negligible dark reversion of phytochrome-far red-absorbing form (Pfr) to phytochrome-red-absorbing form (Pr), and existing as a dimer with an apparent size of approximately 300 kilodaltons”

✓ located verbatim in the source · abstract, characters 567–940

Title

Characterization of Tobacco Expressing Functional Oat Phytochrome

Joel R. Cherry; Howard P. Hershey; Richard D. Vierstra PLANT PHYSIOLOGY 1991. doi:10.1104/pp.96.3.775

Other claims from this paper (10)
Observationobservedoriginal resultmeasured

Claim · model-written summary

The reversible change had maxima at 666 and 730 nm.

Taxon
ZeaZeat0
Outcome
maximum absorbance changese0
Value
666 and 730 nme0

Verbatim

e0

“The difference spectrum of the reversible change showed maximum absorbance changes at 666 and 730 nm”

✓ located verbatim in the source · abstract, characters 285–385
t0

“Zea primary roots”

✓ located verbatim in the source · title, characters 100–117

Title

Photoreversible and photoirreversible absorbance changes in the red and far-red spectral regions in Zea primary roots

Takashi Suzuki; Yukio Shimazaki; Tadashi Fujii; et al. Plant and Cell Physiology 1980. doi:10.1093/oxfordjournals.pcp.a076129

Other claims from this paper (7)
Observationobservedoriginal resultmeasured

Claim · model-written summary

Heat-treated apoperoxidase shows a denaturation blueshift with negative maxima at 287 and 294 nm.

Treatment
heat-treated apoperoxidasee6
Outcome
denaturation blueshifte6
Value
287 and 294 nme6

Verbatim

e0

“Thermal denaturation of Japanese-radish peroxidase”

✓ located verbatim in the source · abstract, characters 0–50
e6

“The difference spectrum of heat-treated apoperoxidase exhibited a denaturation blueshift with negative maxima at 287 and 294 nm, and the total protein fluorescence quantum yield. qprotein, increased by 20% compared to that of the untreated apoenzyme”

✓ located verbatim in the source · abstract, characters 921–1170

Title

Thermal Denaturation and Regeneration of Japanese-radish Peroxidase12

Yoshiyuki TAMURA; Yuhei MORITA The Journal of Biochemistry 1975. doi:10.1093/oxfordjournals.jbchem.a130941

Other claims from this paper (12)
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Heat-treated apoperoxidase shows a 20% increase in total protein fluorescence quantum yield relative to untreated apoenzyme.

Treatment
heat-treated apoperoxidasee6
Outcome
total protein fluorescence quantum yielde6
Direction
increasede6
Value
20%e6
Comparator
untreated apoenzymee6

Verbatim

e0

“Thermal denaturation of Japanese-radish peroxidase”

✓ located verbatim in the source · abstract, characters 0–50
e6

“The difference spectrum of heat-treated apoperoxidase exhibited a denaturation blueshift with negative maxima at 287 and 294 nm, and the total protein fluorescence quantum yield. qprotein, increased by 20% compared to that of the untreated apoenzyme”

✓ located verbatim in the source · abstract, characters 921–1170

Title

Thermal Denaturation and Regeneration of Japanese-radish Peroxidase12

Yoshiyuki TAMURA; Yuhei MORITA The Journal of Biochemistry 1975. doi:10.1093/oxfordjournals.jbchem.a130941

Other claims from this paper (12)
Intervention effectobservedoriginal resultpositivemeasured

Claim · model-written summary

(GlcNAc)3 prevented the NBS oxidation of Trp23 in rye seed chitinase-a.

Treatment
(GlcNAc)3e3
Outcome
oxidatione3
Direction
preventede3
Qualifier
NBS oxidation of Trp23e2

Not reportedComparator

Verbatim

t0

“Rye Seed Chitinase-a”

✓ located verbatim in the source · title, characters 87–107
e2

“The chitin-binding ability of RSC-a was lost upon the NBS oxidation of Trp23 at pH 5.9 or pH 7.0”

✓ located verbatim in the source · abstract, characters 566–662
e3

“This oxidation was prevented by (GlcNAc)3, which induced a high UV-difference spectrum with maxima at 284 and 293 nm”

✓ located verbatim in the source · abstract, characters 664–780

Title

Involvements of Trp23 in the Chitin-binding and of Trp131 in the Chitinase Activity of Rye Seed Chitinase-a

Takeshi Yamagami; Gunki Funatsu Bioscience Biotechnology and Biochemistry 1997. doi:10.1271/bbb.61.1819

Other claims from this paper (12)
Intervention effectobservedoriginal resultpositivemeasured

Claim · model-written summary

NBS oxidation of the isolated Cat domain at pH 5.9 was protected by (GlcNAc)4.

Treatment
(GlcNAc)4e6
Gene
Cat domaine6
Outcome
NBS oxidation of the isolated Cat domaine6
Direction
protectede6
Qualifier
at pH 5.9e6

Not reportedComparator

Verbatim

t0

“Rye Seed Chitinase-a”

✓ located verbatim in the source · title, characters 87–107
e6

“The NBS oxidation of the isolated Cat domain at pH 5.9 was protected by (GlcNAc)4, which induced a UV-difference spectrum with maxima at 284 nm and 293 nm as well as a small trough around 300 nm, similar to that observed in RSC-c”

✓ located verbatim in the source · abstract, characters 1048–1277

Title

Involvements of Trp23 in the Chitin-binding and of Trp131 in the Chitinase Activity of Rye Seed Chitinase-a

Takeshi Yamagami; Gunki Funatsu Bioscience Biotechnology and Biochemistry 1997. doi:10.1271/bbb.61.1819

Other claims from this paper (12)

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