𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle

✍ Scribed by K. Shima; K. Tashiro; N. Hibi; Y. Tsukada; H. Hirai


Publisher
Springer-Verlag
Year
1983
Tongue
English
Weight
807 KB
Volume
59
Category
Article
ISSN
0001-6322

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Characterization of human carbonic anhyd
✍ Nicholas Carter; Stephen Jeffery; Alan Shiels; Yvonne Edwards; Terry Tipler; Dav πŸ“‚ Article πŸ“… 1979 πŸ› Springer 🌐 English βš– 828 KB

A third form of human carbonic anhydrase (CA III), found at high concentrations in skeletal muscle, has been purified and characterized. This isozyme shows relatively poor hydratase and esterase activities compared to the red cell isozymes, CA I and CA II, but is similar to these isozymes in subunit

Leakage of carbonic anhydrase III from n
✍ Dr. HΓ₯kan Ashmark; Dr. Per J. Wistrand πŸ“‚ Article πŸ“… 1992 πŸ› John Wiley and Sons 🌐 English βš– 427 KB

Skeletal muscle extracellular carbonic anhydrase Ill was investigated in anesthetized rats by a microdialysis technique. A small dialysis probe was inserted into the tibialis anterior (TA) muscle and perfused continuously. Perfusates were collected before and during muscle contraction, induced by el

Quantification of carbonic anhydrase III
✍ A. Zheng; P. Rahkila; J. Vuori; S. Rasi; T. Takala; H. K. VÀÀnΓ€nen πŸ“‚ Article πŸ“… 1992 πŸ› Springer 🌐 English βš– 508 KB

Carbonic anhydrase (CA III) and myoglobin contents from isolated human muscle fibers were quantified using a sensitive time-resolved fluoroimmunoassay. Human psoas muscle specimens were freeze-dried, and single fibers were dissected out and classified into type I, IIA and IIB by myosin ATPase staini

Immunohistochemical demonstration of car
✍ T. Kumpulainen πŸ“‚ Article πŸ“… 1983 πŸ› Springer 🌐 English βš– 749 KB

Extravascular location of two main carbonic anhydrase isoenzymes was immunohistochemically investigated in human ciliary processes. The high-activity carbonic anhydrase isoenzyme C was clearly demonstrated in the ciliary epithelium, but was absent from the ciliary stroma. The low-activity isoenzyme