scholarly journals Purification and characterization of the Saccharomyces cerevisiae BGL2 gene product, a cell wall endo-beta-1,3-glucanase.

1993 ◽  
Vol 175 (7) ◽  
pp. 2102-2106 ◽  
Author(s):  
V Mrsa ◽  
F Klebl ◽  
W Tanner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Gene Product ◽  
Purification And Characterization ◽  
A Cell

Purification and characterization of a cell wall proteinase fromStreptococcus lactisNCDO 763

1987 ◽  
Vol 54 (2) ◽  
pp. 247-255 ◽  
Author(s):  
Véronique Monnet ◽  
Dominique Le Bars ◽  
Jean-Claude Gripon
Keyword(s):  
Cell Wall ◽  
Skim Milk ◽  
Serine Proteinase ◽  
Low Ph ◽  
Purification And Characterization ◽  
Streptococcus Lactis ◽  
A Cell ◽  
Cell Wall Extract

SummaryA proteinase was purified from a cell wall extract of a culture ofStreptococcus lactisNCDO 763 grown in skim milk. Being active at a low pH (at pH 4·8 on haemoglobin and pH 6·–6·5 on casein) and completely inhibited by diisopropylfluorophosphate, it was considered to be a serine proteinase partly inhibited by EDTA; the mol. wt was ∼ 80000.

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