𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Partial purification and characterization of a trypsin-like serine protease from bovine sperm

✍ Scribed by Andreina Cesari; Claudio Santiago Cacciato; Rosana Esther De Castro; Jorge Julián Sánchez

Book ID
108785108
Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
192 KB
Volume
27
Category
Article
ISSN
0105-6263

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Crystal structure of bovine duodenase, a
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities
✍ Vladimir Z. Pletnev; Tatyana S. Zamolodchikova; Walter A. Pangborn; William L. D 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 825 KB

The three-dimensional structure of duodenase, a serine protease from bovine duodenum mucosa, has been determined at 2.4A resolution. The enzyme, which has both trypsin-like and chymotrypsin-like activities, most closely resembles human cathepsin G with which it shares 57% sequence identity and simil

Partial purification and characterizatio
Partial purification and characterization of a proteoglycan-degrading neutral protease from bovine epiphyseal cartilage
✍ Dr. Michael G. Ehrlich; Ann L. Armstrong; Henry J. Mankin 📂 Article 📅 1984 🏛 Elsevier Science 🌐 English ⚖ 620 KB

Degradation of the proteoglycan matrix is considered an essential step in the process of calcification in the growth plate. This laboratory has just described the presence of a protease in human growth plate cartilage that degrades proteoglycan at neutral pH. We report here the isolation, partial pu

Presence of a trypsin-like protease in s
Presence of a trypsin-like protease in starfish sperm acrosome
✍ Sousa, Mário ;Moradas-Ferreira, Pedro ;Azevedo, Carlos 📂 Article 📅 1992 🏛 John Wiley and Sons 🌐 English ⚖ 619 KB

## Abstract __Marthasterias glacialis__ sperm cells were treated with ionophore A23187, centrifuged, and the supernatants were assayed for esterase activity. With N‐benzoyl‐L‐arginine ethyl ester‐HCl (BAEE) as substrate, a net activity was determined which was not detectable when N‐acetyl‐L‐tyrosin