Isolation of angiotensin converting enzyme (ACE) binding protein from human serum with an ACE affinity column

1999 ◽  
Vol 77 (3) ◽  
pp. 216-223 ◽  
Author(s):  
Sundararajah Thevananther ◽  
Arthur S Brecher
Keyword(s):  
Molecular Weight ◽  
Angiotensin Converting Enzyme ◽  
Human Serum ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Affinity Column ◽  
Converting Enzyme ◽  
Affinity Ligand ◽  
Human Serum Protein ◽  
Key Enzyme

Immobilized angiotensin-converting enzyme (ACE) was utilized as an affinity ligand to isolate a naturally occurring ACE binding protein from normal human serum. The enzyme was isolated from solubilized bovine lung membrane preparations by lisinopril affinity chromatography. It had an estimated molecular weight of 180 000 and was recognized by the anti-ACE antibody for the rabbit testicular ACE in immunoblots. ACE was immobilized onto epoxy Sepharose as well as Affi-Gel 15. Immobilized ACE on Affi-Gel 15 had higher catalytic activity (0.176 U/mL) compared with the enzyme immobilized on epoxy Sepharose (0.00005 U/mL). Immobilized ACE served as the affinity ligand for the identification of the ACE binding protein in human serum with an estimated molecular weight of 14 000 as observed by SDS polyacrylamide gel electrophoresis. The identification and further characterization of ACE binding proteins in serum and tissues may facilitate the greater understanding of the endogenous regulation of this key enzyme, which is involved in blood pressure homeostasis.Key words: angiotensin-converting enzyme (ACE), ACE binding protein, ACE affinity column, human serum protein.

Angiotensin-converting enzyme signalling in human preadipocytes and adipocytes

2006 ◽  
Vol 1 (2) ◽  
pp. 203-220 ◽  
Author(s):  
Andreas Böttcher ◽  
Alfred Böttcher ◽  
Gerd Schmitz ◽  
Petra Schling
Keyword(s):  
Cell Cycle ◽  
Endothelial Cells ◽  
Angiotensin Converting Enzyme ◽  
Cell Cycle Control ◽  
Converting Enzyme ◽  
Whole Cell Lysate ◽  
Protein Levels ◽  
Adipose Conversion ◽  
Key Enzyme ◽  
Human Preadipocytes

AbstractAngiotensin-converting enzyme (ACE, kininase II) is a plasma membrane zinc metallopeptidase that acts as a key enzyme for the extracellular conversion of vasoactive peptides. Recently, ACE outside-in signalling in endothelial cells has been described. The present study tested the hypothesis that ACE signalling is not restricted to endothelial cells and may act as an additional peptide receptor on human preadipocytes and adipocytes. ACE protein levels were not changed during adipose conversion of human primary preadipocytes. The enzyme was primarily localized to the non-detergent-resistant fraction of the membrane and phosphorylated in non-dividing cells. Antibody arrays of whole cell lysate detected putative ACE-interacting proteins, which all share important roles in cell cycle control and/or apoptosis. These findings suggest that ACE is a versatile molecule, involved both in the regulation of extracellular peptide concentrations and direct intracellular signalling. In human adipose cells ACE may potentially influence exit from the cell cycle, differentiation, and programmed cell death signalling.

scholarly journals The Potential of Hydrolysate from Rabbit Meat Protein as an Angiotensin Converting Enzyme Inhibitor

2019 ◽  
Vol 43 (1) ◽  
Author(s):  
Edy Permadi ◽  
Jamhari Jamhari ◽  
Edi Suryanto ◽  
Zaenal Bachruddin ◽  
Yuny Erwanto
Keyword(s):  
Molecular Weight ◽  
Angiotensin Converting Enzyme ◽  
Soluble Protein ◽  
Ace Inhibitor ◽  
Water Soluble ◽  
Converting Enzyme ◽  
Soluble Protein Content ◽  
Water Soluble Protein ◽  
Rabbit Meat ◽  
Ace Inhibitory

This research aimed to investigate the rabbit meat hydrolysate potential as an angiotensin-converting enzyme (ACE) inhibitor. Indonesian local rabbit meats were used in this study. The research was conducted in Department of Animal Product Technology, Faculty of Animal Science, Universitas Gadjah Mada, from August 2016 to February 2017. The local rabbit meats were hydrolyzed by pepsin, trypsin, and pancreatic. The obtained hydrolysates were then analyzed to identify the water-soluble protein content. The molecular weight of the hydrolysates were also confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The ACE inhibitory properties of the hydrolysates were analyzed in vitro. The results showed that pepsin, trypsin, and pancreatic hydrolysis showed a significant effect on the water-soluble protein content of rabbit meat (p<0.05). The water-soluble protein of rabbit meat hydrolysed by pepsin, trypsin, and pancreatic were 9.41, 7.66, and 9.75 mg/mL respectively. The molecular weight of the rabbit meat hydrolysate were increased from 10 to 43 kDa; 17 to 43 kDa; and 10 to 43 kDa, after hydrolysed by by pepsin, trypsin, and pancreatic respectively. Furthermore, the ACE inhibitory properties ) of the hydrolysed rabbit meat by pepsin, trypsin, and pancreatic were 439, 170, and 380 μg/mL, respectively. The rabbit meat hydrolysate showed a potential to be ACE inhibitor after hydrolyzed with pepsin, trypsin and pancreatic. Moreover, it also showed a promising potential to be used as bioactive components in different pharmaceutical applications. The highest ACE inhibitory capability was showed on trypsin hydrolysis with the total of 65.45% and 170 μg/mL ACE inhibition

scholarly journals Življenje ogrožajoč angioedem po zaviralcu angiotenzinove konvertaze: prikaz dveh primerov Life-threatening angioedema induced by angiotensin-converting enzyme inhibitor: two case reports

2016 ◽  
Vol 84 (12) ◽  
Author(s):  
Erik Rupnik ◽  
Stojan Kariž ◽  
Črtomir Iglič ◽  
Mihaela Zidarn
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Enzyme Inhibitors ◽  
Enzyme Inhibitor ◽  
Case Reports ◽  
Angiotensin Converting Enzyme Inhibitors ◽  
Converting Enzyme ◽  
Converting Enzyme Inhibitors ◽  
Key Enzyme ◽  
Life Threatening

Background. Angioedema is a rare but potentially very serious complication of treatment with angiotensin converting enzyme inhibitors (ACEI). Angioedema is due to the accumulation of bradykinin, because angiotensin converting enzyme is the key enzyme for its degradation.Case reports. We present two patients with life-threatening angioedema while taking ACEI. Both patients had already had episodes of angioedema. Angioedema didn't respond to adrenaline. In both patients intubation was difficult.Conclusion. In the acute phase of angioedema due to ACEI it is necessary to protect the airways. Bradykinin receptor inhibitors shorten the duration of episodes of angioedema. In the long term it is essential to permanently avoid ACEI.

Angiotensin Converting Enzyme Activity in Human Serum: Relationship to Enzyme Inhibitor In Vivo and In Vitro

1982 ◽  
Vol 127 (2) ◽  
pp. 396-396
Author(s):  
B.N. Swanson ◽  
M. Hichens ◽  
P. Mojaverian ◽  
R.K. Ferguson ◽  
P.H. Vlasses ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Angiotensin Converting Enzyme ◽  
Human Serum ◽  
Enzyme Inhibitor ◽  
Converting Enzyme ◽  
Angiotensin Converting Enzyme Activity
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