✦ LIBER ✦

Inhibition of the adenosine-5′-phosphosulfate-sulfotransferase activity from spinach, maize, andChlorellaby adenosine-5′-monophosphate

✍ Scribed by Ahlert Schmidt

Publisher: Springer-Verlag
Year: 1975
Tongue: English
Weight: 161 KB
Volume: 127
Category: Article
ISSN: 0032-0935
DOI: 10.1007/bf00388867

No coin nor oath required. For personal study only.

✦ Synopsis

Adenosin-5'-phosphosulfate (APS) sulfotransferase from higher plants and algae seems to be regulated by adenosine-5'-monophosphate, an endproduct of the APSsulfotransferase reaction. This was found in crude extracts of Spinacea oleracea L. and Zea mays L. and with partially purified APS-sulfotransferase fractions from ChloreUa pyrenoidosa. Half-maximal inhibition with adenosine-5'-monophosphate was found to be (a) 1.3m2V[ for Spinacea; (b) 1.3m2Vl for Zea; and (c) 1.6mM for Chlorella. This inhibition is specific for adenosine-5'-monophosphate, adenosine and adenosine-3'-monophosphate having no inhibitory effect.

📜 SIMILAR VOLUMES

Analysis of the regulation of adenosine

Analysis of the regulation of adenosine 5′-phosphosulfate sulfotransferase activity inLemna minorL. using15N-density labeling

✍ Christoph Arb; Christian Brunold 📂 Article 📅 1980 🏛 Springer-Verlag 🌐 English ⚖ 611 KB

Pyridoxal 5′-phosphate binds to a lysine

Pyridoxal 5′-phosphate binds to a lysine residue in the adenosine 3′-phosphate 5′-phosphosulfate recognition site of glycolipid sulfotransferase from human renal cancer cells

✍ Kouichi Kamio; Koichi Honke; Akira Makita 📂 Article 📅 1995 🏛 Springer US 🌐 English ⚖ 484 KB