✦ LIBER ✦

Differently Labelled Glucosamine-Precursor Pooles for the Biosynthesis of Hyaluronate and Heparan Sulfate

✍ Scribed by Kurt von Figura; Wolfgang Kiowski; Eckhart Buddecke

Book ID: 115113900
Publisher: John Wiley and Sons
Year: 1973
Tongue: English
Weight: 535 KB
Volume: 40
Category: Article
ISSN: 1432-1327
DOI: 10.1111/j.1432-1033.1973.tb03171.x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Isolation of a hyaluronate pool from the

Isolation of a hyaluronate pool from the chondroitin sulfate peptide pool of calf rib cartilage. Effect of puromycin and SeO42− on pool labeling with 3H-glucosamine

✍ Tilmann O. Kleine; B. Merten; H.P. Kirschling 📂 Article 📅 1976 🏛 Elsevier Science ⚖ 455 KB

Biosynthesis of chondroitin sulfate prot

Biosynthesis of chondroitin sulfate proteins isolation of four pools of chondroitin sulfate proteins differing in their solubility and labeling rates with radiosulfate in calf rib cartilage

✍ Tilman O. Kleine; B. Heinrich; K. Goetz 📂 Article 📅 1973 🏛 Elsevier Science 🌐 English ⚖ 328 KB

Interaction between Alzheimer's disease

Interaction between Alzheimer's disease βA4 precursor protein (APP) and the extracellular matrix: Evidence for the participation of heparan sulfate proteoglycans

✍ Jorge Cáceres; Enrique Brandan 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 309 KB 👁 1 views

The interaction between the Alzheimer amyloid precursor protein (APP) and an intact extracellular matrix (ECM), matrigel, obtained from Engelbreth-Holm-Swarm tumors was evaluated. Based on quantitative analyses of the binding data obtained from solid phase binding assays, two binding sites on the EC

Diacylglycerol synthesized in vitro from

Diacylglycerol synthesized in vitro from sn-glycerol 3-phosphate and the endogenous diacylglycerol are different substrate pools for the biosynthesis of phosphatidylcholine in rat lung microsomes

✍ B. Rüstow; D. Kunze 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 525 KB

Acidic and basic fibroblast growth facto

Acidic and basic fibroblast growth factor bind with differing affinity to the same heparan sulfate proteoglycan on BALB/c 3T3 cells: Implications for potentiation of growth factor action by heparin

✍ Kathryn J. Brown; Ian A. Hendry; Christopher R. Parish 📂 Article 📅 1995 🏛 John Wiley and Sons 🌐 English ⚖ 806 KB

Heparan sulfate proteoglycans on the cell surface act as low affinity binding sites for acidic and basic fibroblast growth factor (FGF) [Moscatelli (1987): J Cell Physiol 131:123-1301 and play an important role in the interaction of FGF with the FGF receptor (FGFR). In this study, several aspects of