RT Journal Article SR Electronic(1) A1 Nas, Helga A1 Nissen-Meyer, JonYR 1992 T1 Purification and N-terminal amino acid sequence determination of the cell-wall-bound proteinase from Lactobacillus paracasei subsp. paracasei JF Microbiology, VO 138 IS 2 SP 313 OP 318 DO https://doi.org/10.1099/00221287-138-2-313 PB Microbiology Society, SN 1465-2080, AB SUMMARY: The cell-wall-bound proteinase from Lactobacillus paracasei subsp. paracasei NCDO 151 was purified to homogeneity by anion-exchange and hydrophobic-interaction chromatography, chromatofocusing and gelfiltration. The purification resulted in a 600-700-fold increase in specific activity of the proteinase and the final yield was approximately 20%. Upon chromatofocusing, two proteolytically active components, termed pro 135 and pro110, were detected. pro135 had an isoelectric point of 4·2. It had an M r of about 300000 as determined by gelfiltration and 135000 as judged by SDS-PAGE, indicating that it may exist as a dimer in its native state, pro110 had an isoelectric point of 4·4, and an M r of about 150000 as determined by gel-filtration and 110000 as judged by SDS-PAGE. pro110 appears to be a degradation product of pro135 as they have the same N-terminal amino acid sequence. The first N-terminal amino acid was ambiguous for both components, whereas the sequence from the second to the ninth amino acid was Ala-Lys-Ala-Asn-Ser-Met-Ala-Asn. This is identical to the corresponding sequence of the lactococcal cell-wall-bound proteinases. Although the Lactobacillus proteinase was a little smaller than the lactococcal proteinase, their purification characteristics were very similar, suggesting that these proteinases are related., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-138-2-313