Selective isolation of bacteria with dipeptidyl aminopeptidase type I activity from the sheep rumen

Nest McKain, R. John Wallace, Nicola D. Watt

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Five-hundred-and-six fresh isolates of rumen bacteria were tested for their ability to hydrolyse the synthetic substrate for dipeptidyl aminopeptidase type I, GlyArg-4-methoxy-2-naphthylamide (GlyArg-MNA), using a gel overlay technique. Twelve positive isolates were small Gram-negative rods which resembled Bacteroides ruminicola in their biochemical and morphological properties. SDS-PAGE of whole cell extracts indicated that two were similar to B. ruminicola strain B14, six resembled B. ruminicola strain M384, and four were similar to B. ruminicola GA33. All hydrolysed GlyArg-MNA, Ala2 and Ala5, and showed no activity against Leu-MNA. Ala3 and Ala2, but no Ala4, was produced from Ala5. The different groups had different, distinctive activity profiles. The two remaining positive isolates were Lactobacillus spp. with an exceptionally high Leu-MNA activity. It was concluded that, although different strains may only be distantly related, B. ruminicola forms the most important group of bacteria in the rumen to possess a dipeptidyl aminopeptidase type I activity.
Original languageEnglish
Pages (from-to)169-174
Number of pages6
JournalFEMS Microbiology Letters
Volume95
Issue number2-3
DOIs
Publication statusPublished - 15 Aug 1992

Fingerprint

Cathepsin C
Rumen
Sheep
Bacteria
Bacteroides
Lactobacillus
Cell Extracts
Polyacrylamide Gel Electrophoresis
Gels
2-naphthylamide

Cite this

Selective isolation of bacteria with dipeptidyl aminopeptidase type I activity from the sheep rumen. / McKain, Nest; Wallace, R. John; Watt, Nicola D.

In: FEMS Microbiology Letters, Vol. 95, No. 2-3, 15.08.1992, p. 169-174.

Research output: Contribution to journalArticle

@article{e9c3186a4f18437b8b0b32e0583cd7fb,
title = "Selective isolation of bacteria with dipeptidyl aminopeptidase type I activity from the sheep rumen",
abstract = "Five-hundred-and-six fresh isolates of rumen bacteria were tested for their ability to hydrolyse the synthetic substrate for dipeptidyl aminopeptidase type I, GlyArg-4-methoxy-2-naphthylamide (GlyArg-MNA), using a gel overlay technique. Twelve positive isolates were small Gram-negative rods which resembled Bacteroides ruminicola in their biochemical and morphological properties. SDS-PAGE of whole cell extracts indicated that two were similar to B. ruminicola strain B14, six resembled B. ruminicola strain M384, and four were similar to B. ruminicola GA33. All hydrolysed GlyArg-MNA, Ala2 and Ala5, and showed no activity against Leu-MNA. Ala3 and Ala2, but no Ala4, was produced from Ala5. The different groups had different, distinctive activity profiles. The two remaining positive isolates were Lactobacillus spp. with an exceptionally high Leu-MNA activity. It was concluded that, although different strains may only be distantly related, B. ruminicola forms the most important group of bacteria in the rumen to possess a dipeptidyl aminopeptidase type I activity.",
author = "Nest McKain and Wallace, {R. John} and Watt, {Nicola D.}",
note = "91",
year = "1992",
month = "8",
day = "15",
doi = "10.1016/0378-1097(92)90424-M",
language = "English",
volume = "95",
pages = "169--174",
journal = "FEMS Microbiology Letters",
issn = "0378-1097",
publisher = "Oxford University Press",
number = "2-3",

}

TY - JOUR

T1 - Selective isolation of bacteria with dipeptidyl aminopeptidase type I activity from the sheep rumen

AU - McKain, Nest

AU - Wallace, R. John

AU - Watt, Nicola D.

N1 - 91

PY - 1992/8/15

Y1 - 1992/8/15

N2 - Five-hundred-and-six fresh isolates of rumen bacteria were tested for their ability to hydrolyse the synthetic substrate for dipeptidyl aminopeptidase type I, GlyArg-4-methoxy-2-naphthylamide (GlyArg-MNA), using a gel overlay technique. Twelve positive isolates were small Gram-negative rods which resembled Bacteroides ruminicola in their biochemical and morphological properties. SDS-PAGE of whole cell extracts indicated that two were similar to B. ruminicola strain B14, six resembled B. ruminicola strain M384, and four were similar to B. ruminicola GA33. All hydrolysed GlyArg-MNA, Ala2 and Ala5, and showed no activity against Leu-MNA. Ala3 and Ala2, but no Ala4, was produced from Ala5. The different groups had different, distinctive activity profiles. The two remaining positive isolates were Lactobacillus spp. with an exceptionally high Leu-MNA activity. It was concluded that, although different strains may only be distantly related, B. ruminicola forms the most important group of bacteria in the rumen to possess a dipeptidyl aminopeptidase type I activity.

AB - Five-hundred-and-six fresh isolates of rumen bacteria were tested for their ability to hydrolyse the synthetic substrate for dipeptidyl aminopeptidase type I, GlyArg-4-methoxy-2-naphthylamide (GlyArg-MNA), using a gel overlay technique. Twelve positive isolates were small Gram-negative rods which resembled Bacteroides ruminicola in their biochemical and morphological properties. SDS-PAGE of whole cell extracts indicated that two were similar to B. ruminicola strain B14, six resembled B. ruminicola strain M384, and four were similar to B. ruminicola GA33. All hydrolysed GlyArg-MNA, Ala2 and Ala5, and showed no activity against Leu-MNA. Ala3 and Ala2, but no Ala4, was produced from Ala5. The different groups had different, distinctive activity profiles. The two remaining positive isolates were Lactobacillus spp. with an exceptionally high Leu-MNA activity. It was concluded that, although different strains may only be distantly related, B. ruminicola forms the most important group of bacteria in the rumen to possess a dipeptidyl aminopeptidase type I activity.

U2 - 10.1016/0378-1097(92)90424-M

DO - 10.1016/0378-1097(92)90424-M

M3 - Article

VL - 95

SP - 169

EP - 174

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

SN - 0378-1097

IS - 2-3

ER -