𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Ca-activated neutral protease and its inhibitors: In vitro effect on intact myofibrils

✍ Scribed by Dr. Hideo Sugita; Dr. Shoichi Ishiura; Dr. Koichi Suzuki; Dr. Kazutomo Imahori

Publisher
John Wiley and Sons
Year
1980
Tongue
English
Weight
489 KB
Volume
3
Category
Article
ISSN
0148-639X

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Effects of thiol protease inhibitors on
Effects of thiol protease inhibitors on myoblast fusion and myofibril assembly in vitro
✍ Moncman, Carole L. ;Wang, Kuan 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 907 KB

To investigate the roles of thiol proteases such as cathepsins and calpains in muscle differentiation, we have treated primary cultures of pectoralis muscle with a variety of protease inhibitors and examined the effects these agents have on myoblast fusion and myofibrillogenesis. We have found that

The effect of serine and thiol protease
The effect of serine and thiol protease inhibitors on the chemiluminescence of human neutrophils in investigationsIn Vitro
✍ Kantorski, J. ;Tchórzewski, H. 📂 Article 📅 1992 🏛 John Wiley and Sons ⚖ 563 KB

We have studied an indirect role of serine and thiol proteases in the activation of human neutrophils in vitro. Stimulation was evaluated using a chemiluminescence (CL) generation system. Receptor-dependent and receptor-independent stimuli were studied, e.g. opsonized zymosan, formyl-methionyl-leucy

In vitro adsorption of diphenoxylate hyd
In vitro adsorption of diphenoxylate hydrochloride on activated charcoal and its relationship to pharmacological effects of drug in vivo I
✍ Dilip R. Sanvordeker; Esam Z. Dajani 📂 Article 📅 1975 🏛 John Wiley and Sons 🌐 English ⚖ 347 KB 👁 1 views

The adsorption of diphenoxylate hydrochloride, a POtent antidiarrheal agent, on activated charcoal powder was studied in uitro. Langmuir adsorption isotherms were established a t pH 4 and 7, and the maximum adsorption capacity of charcoal for this drug was estimated using these values. Activated cha

Activation of Src kinase by protein–tyro
Activation of Src kinase by protein–tyrosine phosphatase–PEST in osteoclasts: Comparative analysis of the effects of bisphosphonate and protein–tyrosine phosphatase inhibitor on Src activation in vitro
✍ Meenakshi A. Chellaiah; Michael D. Schaller 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 403 KB 👁 2 views

## Abstract PTP–PEST is involved in the regulation of sealing ring formation in osteoclasts. In this article, we have shown a regulatory role for PTP–PEST on dephosphorylation of c‐Src at Y527 and phosphorylation at Y418 in the catalytic site. Activation of Src in osteoclasts by over‐expression of