𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Hyperthermic “dose” dependent changes in intralesional pH

✍ Scribed by Fred W. Hetzel; Kurt Avery; Michael Chopp


Publisher
Elsevier Science
Year
1989
Tongue
English
Weight
389 KB
Volume
16
Category
Article
ISSN
0360-3016

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Light-dependent pH changes in leaves of
✍ Zu-Hua Yin; Spidola Neimanis; Ulrich Heber 📂 Article 📅 1990 🏛 Springer-Verlag 🌐 English ⚖ 886 KB

Illumination of leaves of C 3 plants caused cytosolic alkalization and vacuolar acidification in the mesophyll cells. Both phenomena were particularly pronounced when CO2 was absent, were suppressed by CO2, and were related to the activation state of the photosynthetic apparatus. The cytosolic alkal

Light-dependent pH changes in leaves of
✍ Zu-Hua Yin; Karl-Josef Dietz; Ulrich Heber 📂 Article 📅 1990 🏛 Springer-Verlag 🌐 English ⚖ 817 KB

Etiolated leaves and the inhibitors of photosynthesis 3-(3,4-dichlorophenyl)-l,l-dimethylurea (DCMU) and oL-glyceraldehyde were used to study the relationship between thylakoid energization, photosynthesis, the light-dependent alkalization of the cytosol of mesophyll cells and the acidification of m

Light-dependent pH changes in leaves of
✍ Zu-Hua Yin; Katharina Siebke; Ulrich Heber 📂 Article 📅 1991 🏛 Springer-Verlag 🌐 English ⚖ 528 KB

Action spectra in the red region of the spectrum for light-dependent cytosolic alkalization in leaves of C3 plants which also received a low background of blue light differed from the action spectra for light-dependent vacuolar acidification. Light above 680 nm was less effective in supporting the c

pH dependent conformational changes and
✍ E. L. Gross; J. E. Draheim; G. P. Anderson; D. G. Sanderson; S. L. Ketchner 📂 Article 📅 1986 🏛 Springer 🌐 English ⚖ 371 KB

Reduction of plastocyanin (PC) caused a change in the electric field at the surface of the molecule which resulted in a 0.3 pH unit increase in the pKa of a nitrated derivative of Tyr 83. This change in electrical potential could alter the affinity for cytochrome f which is known to bind at this sit