scholarly journals Purification and Properties of Pancreatic Juice Cholesterol Esterase

1969 ◽  
Vol 244 (7) ◽  
pp. 1937-1945 ◽  
Author(s):  
J Hyun ◽  
H Kothari ◽  
E Herm ◽  
J Mortenson ◽  
C R Treadwell ◽  
...  
1972 ◽  
Vol 152 (1) ◽  
pp. 233-242 ◽  
Author(s):  
J. Hyun ◽  
C.R. Treadwell ◽  
G.V. Vahouny

1979 ◽  
Vol 27 (7) ◽  
pp. 1704-1707 ◽  
Author(s):  
TOSHIO KAMEI ◽  
HAJIME SUZUKI ◽  
KAZUKO ASANO ◽  
MEIKI MATSUZAKI ◽  
SHOSHIRO NAKAMURA

1991 ◽  
Vol 37 (3) ◽  
pp. 361-368 ◽  
Author(s):  
John A Lott ◽  
Carrle J Lu

Abstract Pancreatic juice and serum from patients with acute pancreatitis contain three enzymes that have lipolytic activity: L1 and L2, which are pancreatic isoenzymes or isoforms of lipase (EC 3.1.1.3), and L3, which is probably pancreatic carboxyl ester lipase, also known as cholesterol esterase (EC 3.1.1.13). These enzymes are readily separated electrophoretically on agarose and can be developed with an overlay of Kodak Ektachem lipase slide material. The latter acts as a dry-reagent developing substrate, with the enzymes producing blue bands in the slide material. We found L1 in about one-half of normal persons, L2 in none, and L3 in all. We assayed for amylase (EC 3.2.1.1), amylase isoenzymes, lipase, and lipase isoforms in the sera of 100 patients with suspected acute pancreatitis. L2 lipase has the greatest diagnostic efficiency for the diagnosis of pancreatitis, compared with total amylase, P3 amylase, and total lipase. Lipase and L2 could replace amylase, an inefficient test, for the diagnosis of patients with suspected acute pancreatitis. In patients receiving organ transplants, a serum amylase value of greater than 300 U/L or a lipase of greater than 1000 U/L discriminated well between patients with and without complications and (or) acute rejection.


1964 ◽  
Vol 206 (1) ◽  
pp. 223-228 ◽  
Author(s):  
C. R. Borja ◽  
George V. Vahouny ◽  
C. R. Treadwell

Absence of bile and pancreatic juice in the intestinal tract totally abolished absorption of cholesterol-4-C14 into thoracic duct lymph. Similarly, intestinal cholesterol esterase activity approached zero in animals lacking both bile and pancreatic juice. Intestinal cholesterol esterase could still be demonstrated in animals deprived of pancreatic juice, but which received an infusion or intragastric administration of bile salts. Absorption of cholesterol was shown to occur even in the complete absence of pancreatic juice, provided bile salts were present in the intestinal tract. Some synthesis of cholesterol esterase by the intestinal or reactivation of residual cholesterol esterase in the presence of bile salts is postulated. Thus, pancreatic secretion is not absolutely required for cholesterol absorption, although it has a stimulating effect in the presence of bile salts. This effect is attributed to its cholesterol esterase content. In the presence of bile salts, the process of esterification is postulated to be a rate-limiting step during intestinal absorption of dietary cholesterol.


1971 ◽  
Vol 25 ◽  
pp. 577-589 ◽  
Author(s):  
Bo Arnesjö ◽  
Anders Grubb ◽  
Gustav Schroll ◽  
A. A. Lindberg ◽  
Inger Lagerlund ◽  
...  

1982 ◽  
Vol 10 (4) ◽  
pp. 747-750
Author(s):  
Tsuneo IMANAKA ◽  
Kimiko MUTO ◽  
Yoshinori MORIYAMA ◽  
Shoji OHKUMA ◽  
Tatsuya TAKANO

1981 ◽  
Vol 91 (3) ◽  
pp. 344-346 ◽  
Author(s):  
I. M. Karmanskii ◽  
A. L. Pichugin ◽  
G. I. Yusupova ◽  
Yu. A. Sysoev

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