Topic
Proteolytic enzymes
About: Proteolytic enzymes is a research topic. Over the lifetime, 23096 publications have been published within this topic receiving 835544 citations.
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TL;DR: In this paper, inosine and hypoxanthine were found to be dialyzable, heat stable, and resistant to degradation by proteolytic enzymes, and further purification by gel filtration, ion exchange chromatography, thin-layer chromatography and high pressure liquid chromatography demonstrated that these compounds are inOSINE and hypoxideanthine.
174 citations
TL;DR: It is shown by complementation that the gacA gene is also essential for the expression of two extracellular enzymes in P. fluorescens CHA0: phospholipase C and a 47-kDa metalloprotease.
Abstract: Pseudomonas fluorescens strain CHA0 protects plants from various root diseases. Antibiotic metabolites synthesized by this strain play an important role in disease suppression; their production is mediated by the global activator gene gacA. Here we show by complementation that the gacA gene is also essential for the expression of two extracellular enzymes in P. fluorescens CHA0: phospholipase C and a 47-kDa metalloprotease. In contrast, the production of another exoenzyme, lipase, is not regulated by the gacA gene. Protease, phospholipase and antibiotics of P. fluorescens are all known to be optimally produced at the end of exponential growth; thus, the gacA gene appears to be a general stationary-phase regulator.
174 citations
TL;DR: Specific spots in the complex cytoplasmic protein gel pattern which corresponded to the initiation factor proteins were identified by co-migration of purified initiation factors with 35S-labeled cell lysates, partial proteolytic digestion mapping, and immunoblotting analysis using antisera or affinity-purified antibodies to the initiated factors.
174 citations
Journal Article•
TL;DR: It is concluded that human trophoblasts can express both PAI-1 andPAI-2 in vitro and in vivo and prominent PAI -1 immunostaining defines invading trophoblastasts, whereas PAi-2 is the predominant PAI accumulated in villous syncytiotrophoblasts.
174 citations
TL;DR: A BamHI-generated chloroplast DNA sequence cloned in Escherichia coli is shown to direct the in vitro synthesis of this protein identified as large subunit by its size, serological properties, and limited proteolytic digestion products.
Abstract: In vitro linked transcription-translation of chloroplast DNA has been used to show that the large subunit of ribulose-1,5-bisphosphate carboxylase [3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] is encoded by Zea mays chloroplast DNA. A BamHI-generated chloroplast DNA sequence cloned in Escherichia coli is shown to direct the in vitro synthesis of this protein identified as large subunit by its size, serological properties, and limited proteolytic digestion products.
174 citations