ArticleThe Biochemical journal1989
Cloning and expression of human salivary-gland kallikrein in Escherichia coli.
Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 26 citations in OpenAlex.
- Crystal structure of recombinant human tissue kallikrein at 2.0 A resolution.Protein science : a publication of the Protein Society · 1998Article
- A novel protease homolog differentially expressed in breast and ovarian cancer.Molecular medicine (Cambridge, Mass.) · 1996Article
- Purification and characterization of recombinant tissue kallikrein from Escherichia coli and yeast.The Biochemical journal · 1991Article
- New nucleotide sequence data on the EMBL File Server.Nucleic acids research · 1990Article
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
CDNA clones for human kallikrein have been identified in a cDNA library constructed from mRNA of human salivary gland. The entire coding sequence for preprokallikrein and for the 5'- and 3'-untranslated regions were isolated by using a mixture of oligonucleotides corresponding to amino acids 51-56 of human urinary kallikrein and one oligonucleotide corresponding to amino acids 233-238 of human pancreatic kallikrein. The DNA sequence proved that, with the exception of two amino acid exchanges, kallikrein of the human salivary gland is identical with pancreatic kallikrein. Salivary gland and renal kallikrein was expressed in Escherichia coli from plasmid pKK223-3 under the control of the tac promoter. The protein was identified by Western-blot analysis and by demonstration of its specific proteolytic activity.
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Registered trials
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