ArticleThe Biochemical journal2000
Purification of Golgi casein kinase from bovine milk.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- Binding of Clostridium botulinum C3 exoenzyme to intact cells.Naunyn-Schmiedeberg's archives of pharmacology · 2014Article
- FAM20C functions intracellularly within both ameloblasts and odontoblasts in vivo.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2013Article
- Secreted protein kinases?Trends in biochemical sciences · 2013Article
- Secreted protein kinases.Trends in biochemical sciences · 2013Review
- Secreted kinase phosphorylates extracellular proteins that regulate biomineralization.Science (New York, N.Y.) · 2012Article
- Paradigm-shifters: phosphorylated prolactin and short prolactin receptors.Journal of mammary gland biology and neoplasia · 2008Review
- The ABCs of the atypical Fam20 secretory pathway kinases.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caseins and many other secretory proteins are phosphorylated during their transport through the secretory pathway by a protein kinase present within Golgi compartments. Molecular analysis of the Golgi casein kinase (GCK) has not been possible since it has not been purified to homogeneity or been cloned. Previous attempts have been made to purify GCK activity from mammary gland Golgi fractions, but these have not resulted in extensive purification of the enzyme. In the present study, we have demonstrated that substantial amounts of GCK activity, assayed using a specific peptide substrate, can be detected as a soluble form in bovine milk, and we have used milk as a source for purification. A purification protocol was established that allowed>80000-fold purification to a specific activity of GCK (approx. 700 nmoles/min per mg of protein) far higher than previously achieved. These findings cast doubts on previous claims for purification of GCK activity. In addition, ion-exchange chromatography resolved two closely eluting peaks of activity, suggesting the existence of two related, but distinct, GCK activities.
Indexed as
Identifiers
10947960PMC1221273W2090028296What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.