✦ LIBER ✦

Isolation and characterization of the digestive proteinases in the earthworm Lumbricus terrestris Linnaeus

✍ Scribed by Glenn C. Bewley; Edward J. DeVillez

Book ID: 115830532
Publisher: Elsevier Science
Year: 1968
Weight: 737 KB
Volume: 25
Category: Article
ISSN: 0010-406X
DOI: 10.1016/0010-406x(68)90591-4

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Isolation, purification and partial char

Isolation, purification and partial characterization of chloragocytes from the earthworm species Lumbricus terrestris

✍ E.B. Affar; M. Dufour; G.G. Poirier; D. Nadeau 📂 Article 📅 1998 🏛 Springer 🌐 English ⚖ 368 KB

Fate of Protozoa transiting the digestiv

Fate of Protozoa transiting the digestive tract of the earthworm Lumbricus terrestris L.

✍ Houjian Cai; Boris Zarda; Geoffrey R. Mattison; Frank Schönholzer; Dittmar Hahn 📂 Article 📅 2002 🏛 Elsevier Science 🌐 English ⚖ 348 KB

Temperature and conditioning in the eart

Temperature and conditioning in the earthworm, Lumbricus terrestris

✍ Michael J. Herz; Harman V.S. Peeke; Everett J. Wyers 📂 Article 📅 1964 🏛 Elsevier Science 🌐 English ⚖ 431 KB

Changes in the fatty acid profiles throu

Changes in the fatty acid profiles through the digestive tract of the earthworm Lumbricus terrestris L.

✍ Luis Sampedro; Joann K. Whalen 📂 Article 📅 2007 🏛 Elsevier Science 🌐 English ⚖ 399 KB

Occurrence of ceramide-glycanase in the

Occurrence of ceramide-glycanase in the earthworm, Lumbricus terrestris

✍ Yu-Teh Li; Yukitoshi Ishikawa; Su-Chen Li 📂 Article 📅 1987 🏛 Elsevier Science 🌐 English ⚖ 443 KB

Metabolic sources of ammonia in the eart

Metabolic sources of ammonia in the earthworm,Lumbricus terrestris L

✍ MacDonnell, Paul C. ;Tillinghast, Edward K. 📂 Article 📅 1973 🏛 John Wiley and Sons 🌐 English ⚖ 530 KB

## Abstract The earthworm __Lumbricus terrestris__ is ammonotelic while feeding but becomes ureotelic with fasting. The metabolic sources of ammonia nitrogen in feeding worms have been examined. Two deaminating enzymes, L‐serine dehydratase and 5′‐AMP deaminase, have been observed to be present in