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Query: UMLS:C0162871 (
abdominal aortic aneurysm
)
8,664
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
To assess the diagnostic value of
myoglobin
between elective surgery and acute arterial occlusion, serum and urine
myoglobin
(S-Mb, U-Mb) levels were measured before and for 7 consecutive days following arterial reconstructive surgery in 7 patients with
abdominal aortic aneurysm
or arteriosclerosis obliterans (elective surgery group), and in 20 patients with acute arterial occlusion due to embolism or thrombosis. They were divided into three groups based on symptoms and other features: mild, moderate, and severe groups. S-Mb and U-Mb levels were normal before surgery with a maximum of 389 ng/ml and 1,670 ng/ml after surgery in the elective surgery group, and 489 ng/ml and 11.7 ng/ml before surgery with a maximum of 703 ng/ml and 294 ng/ml after surgery in the mild cases. These two groups showed no complications after surgery. In the moderate group, high values of 2,420 ng/ml and 25,300 ng/ml were noted before surgery, and these values were elevated to 14,900 ng/ml and 175,000 ng/ml after surgery with complications of acute renal failure or peripheral nerve paresis. In the severe group, the values were 9,440 ng/ml and 260,000 ng/ml before surgery, and 160,000 ng/ml and 1,300,000 ng/ml after surgery, the elevation being associated with the severe clinical complication, myonephropathic metabolic syndrome (MNMS). All patients in this group died of MNMS. S-Mb and U-Mb levels before surgery proved useful for predicting the prognosis of patients with acute arterial occlusion. The findings obtained in our canine studies on the mechanism and treatment of MNMS suggest that alpha-tocopherol, a free radical scavenger, may be effective for treating dreadful complications such as MNMS.
...
PMID:[Arterial reconstructive surgery and myoglobin]. 204 Dec 11
A 66-year-old man underwent emergency surgery for a ruptured
abdominal aortic aneurysm
associated with right common and internal iliac aneurysms. Postoperatively, his right buttock was distended and tender to compression. A CT scan revealed an extremely swollen right gluteus maximus with decreased density. Macromyoglobinuria was noted, and creatine kinase and
myoglobin
were elevated: 87,800 IU/l and 144,300 ng/ml, respectively. Renal function had deteriorated and he was treated with hemodialysis until the 15th postoperative day. The patient recovered without any discomfort to the buttock or intermittent claudication. To our knowledge this is the first documented case of gluteal compartment syndrome after the repair of an
abdominal aortic aneurysm
.
...
PMID:Gluteal compartment syndrome after abdominal aortic aneurysm repair. 1522 62
To characterize the roles played by surface-charged residue Asp44 in the structure stability of horse heart
myoglobin
, the code of Asp44, GAT, in the gene of horse heart
myoglobin
was changed into
AAA
for Lys by PCR site-directed mutagenesis. The mutant gene was ligated into PstI/BamHI-cut pGYM and the resulting plasmid was transformed into E. coli BL21. The mutant protein (D44K) was expressed in BL21 successfully. The bacteria containing mutant
myoglobin
were treated with lysozyme. Then the mutant protein was purified by ammonium sulfate precipitation, ion-exchange chromatography and gel filtration. Circular dichroism spectra were employed to monitor the kinetic behaviors of wild-type and mutant myoglobins' denaturation at different pHs or upon heating, and the "two-state" model was used to simulate the kinetic process of wild-type and mutant myoglobins' denaturation upon heating to determine the unfolding thermodynamic parameters of Mb and its mutant (D44K). The results show that the mutation of the surface-charged residue Asp44 to Lys44 can increase the protein's stability on its resistance to heat, resulting in the increase in the protein's denaturing mid-temperature by about 4 degrees C, from 71.9 to 75.1 degrees C, but shows little effect on its resistance to acid denaturation.
...
PMID:[Probe of the effect of Asp44 on the stability of myoglobin by circular dichroism spectropolarimeter]. 1847 38