1963
DOI: 10.1038/200901a0
|View full text |Cite
|
Sign up to set email alerts
|

Acetylcholinesterase Inactivation of Enzymetreated Erythrocytes

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

3
25
0

Year Published

1968
1968
2016
2016

Publication Types

Select...
7
1

Relationship

2
6

Authors

Journals

citations
Cited by 60 publications
(28 citation statements)
references
References 10 publications
3
25
0
Order By: Relevance
“…The failure to restore enzyme activity by repeated washing of the antibiotic-treated cells indicated that the effect was irreversible, thereby resembling the inactivating action observed with benzylpenicillin [10]. The present findings are also reminiscent of the effects of proteases [7] and of tannic acid [20] on erythrocyte enzymes; that is, only the membrane associated ACHE, but not the intracellularly located G6PD was destroyed when whole red cells were exposed to the antibiotic. These observations suggest that cephalothin only interacts with specific segments of the outer surface of the human erythrocyte.…”
Section: Discussionsupporting
confidence: 57%
See 2 more Smart Citations
“…The failure to restore enzyme activity by repeated washing of the antibiotic-treated cells indicated that the effect was irreversible, thereby resembling the inactivating action observed with benzylpenicillin [10]. The present findings are also reminiscent of the effects of proteases [7] and of tannic acid [20] on erythrocyte enzymes; that is, only the membrane associated ACHE, but not the intracellularly located G6PD was destroyed when whole red cells were exposed to the antibiotic. These observations suggest that cephalothin only interacts with specific segments of the outer surface of the human erythrocyte.…”
Section: Discussionsupporting
confidence: 57%
“…However, studies with red cells separated in accordance with their density revealed that in this disorder the enzyme distribution pattern was characteristically different than that found in ABO hemolytic disease [6]. Investigations undertaken to elucidate the pathophysiology of this enzyme defect have shown that alterations of ACHE activity can be produced by exposing normal erythrocytes to certain chemically-unrelated sub stances which interact with the red cell membrane [7][8][9]. From in activation studies with proteolytic enzymes it has been inferred that ACHE appears to be located at the outer surface of the human erythrocyte [5].…”
mentioning
confidence: 99%
See 1 more Smart Citation
“…A similar enzyme defect has been detected in red cells of patients with paroxysmal nocturnal hemo globinuria (PNH) (2,3). Alterations of ACHE activity can also be produced artificially by treating normal erythrocytes with proteo lytic enzymes (4,5) and with certain sulfhydryl reagents (6).…”
mentioning
confidence: 89%
“…However, an exception is seen in pa- Brauer and Root [11] in 1945 showed that after in vitro hemolysis, acetylcholinesterase activity can be recovered in the erythrocyte membrane. Studies with proteolytic enzymes, which are unable to traverse the erythrocyte membrane, have indicated that acetylcholinesterase or its active sites are located at or near the outer surface of the human erythrocyte [7,30,51,74]. It has been suggested on the basis of a molecular weight of 90,000 or 180,000/active site that 0.2% of human erythrocyte membrane proteins is active acetylcholinesterase [6].…”
Section: Acetylcholinesterase In the Erythrocytementioning
confidence: 99%