{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T07:53:40Z","timestamp":1767167620394,"version":"build-2238731810"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[1973,3,1]],"date-time":"1973-03-01T00:00:00Z","timestamp":99792000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Microbiol"],"published-print":{"date-parts":[[1973,3]]},"abstract":"<jats:p>\n                    Proteins in sonic extracts of\n                    <jats:italic>Streptococcus lactis<\/jats:italic>\n                    were separated by starch-gel electrophoresis at high voltage. Each slab was sliced longitudinally, and half was stained for peptidases in a mixture containing a peptide, L-amino acid oxidase (snake venom), peroxidase, and\n                    <jats:italic>o<\/jats:italic>\n                    -dianisdine; the other half was stained in amido black for protein. In addition to sonic treatment, trypsin also released enzyme from acetone-treated cells. Glycyl-L-phenylalanine, L-phenylalanyl-glycine, L-alanyl-L-phenylalanine, and L-phenylalanyl-L-alanine served as substrates in characterizing the enzymes. Five different fractions of various specificities appeared in the gels. Broad-range substrate specificities were found for sonic extracts of\n                    <jats:italic>S. lactis, S. cremoris, S. durans<\/jats:italic>\n                    , and\n                    <jats:italic>Lactobacillus acidophilus<\/jats:italic>\n                    .\n                  <\/jats:p>","DOI":"10.1128\/am.25.3.388-395.1973","type":"journal-article","created":{"date-parts":[[2020,12,5]],"date-time":"2020-12-05T03:39:50Z","timestamp":1607139590000},"page":"388-395","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["Fractionation of Dipeptidase Activities of\n                    <i>Streptococcus lactis<\/i>\n                    and Dipeptidase Specificity of Some Lactic Acid Bacteria"],"prefix":"10.1128","volume":"25","author":[{"given":"Terje","family":"S\u00f8rhaug","sequence":"first","affiliation":[{"name":"Agricultural University of Norway, \u00c5s-NLH 1432, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter","family":"Solberg","sequence":"additional","affiliation":[{"name":"Agricultural University of Norway, \u00c5s-NLH 1432, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","container-title":["Applied Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/am.25.3.388-395.1973","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/am.25.3.388-395.1973","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,23]],"date-time":"2022-02-23T08:46:17Z","timestamp":1645605977000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/am.25.3.388-395.1973"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1973,3]]},"references-count":0,"aliases":["10.1128\/aem.25.3.388-395.1973"],"journal-issue":{"issue":"3","published-print":{"date-parts":[[1973,3]]}},"alternative-id":["10.1128\/am.25.3.388-395.1973"],"URL":"https:\/\/doi.org\/10.1128\/am.25.3.388-395.1973","relation":{},"ISSN":["0003-6919"],"issn-type":[{"value":"0003-6919","type":"print"}],"subject":[],"published":{"date-parts":[[1973,3]]},"assertion":[{"value":"1973-03-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}