angiotensin II

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a potent vasopressor agent formed from angiotensin I

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References in periodicals archive ?
Objective: (1(b)) Subject to: (2(a)), (5(a-i)), (6(a-i)), (6(a-ii)), (7(a)), (10(a)), (10(b)), (12(a)) and (12(b)).
MTSC-2: Objective: (1(b)) Subject to: (2(a)), (3(a-i)), (3(a-ii)), (4(a)), (5(a-i)), (5(a-ii)), (6(a-i)), (6(a-ii)), (7(a)), (10(a)), (10(b)), (12(a)) and (12(b)).
MTSC-3: Objective: (1(b)) Subject to: (2(a)), (3(a-i)), (3(a-ii)), (5(a-i)), (5(a-ii)), (6(a-i)), (6(a-ii)), (7(a)), (9(a)), (9(b)), (10(a)), (10(b)), (12(a)) and (12(b)).
MTSC-LR-1: Dualize (2(a)), (5(a-i)), (6(a-i)), (6(a-ii)).
Subject to: (3(a-i)), (3(a-ii)), (5(a-ii)), (7(a)), (8(a)), (8(b)), (9(a)), (9(b)), (10(a)), (10(b)).
The geographical distribution of the five major [beta]-amylase types (A-II, B-I, B-Ia, B-II, and CII) in the world is shown in Fig.
From the east to west, the ratio of the A-II type accessions gradually decreased, the lowest ratio being found in Turkey (0.8%) and Ethiopia (0.7%), while the ratios of the B-Ia and C-II type accessions increased.
In Mongolia, the ratio of [beta]-amylase types seems to reflect the influence of barley germplasm from its neighbors: the C-II allele was from the former USSR and the A-II allele was mainly from China.
In conclusion, on the basis of the classification of [beta]-amylase types, cultivated barley could be divided into five major types from five respective centers of origin in the world: A-II type barley center was in East Asia, B-I type center was in North Europe, B-Ia type center was in the Middle East and Southwest Asia, B-II type barley was spread from Turkey, and the C-II type center was in Ethiopia.
Western blot analysis revealed staining of 2 protein bands at approximately [M.sub.r] 17 000 and [M.sub.r] 34 000 by anti-APO A-II antibody.
The observed increase in APO A-II in CSF of brain tumor patients might be the result of protein leakage from the blood to the CSF attributable to a disrupted blood-brain barrier.
The albumin concentration in CSF was significantly (P <0.0001) correlated with the peak intensities of the 2 protein peaks in the m/z 17 000 APO A-II protein cluster in our SELDI experiments (Fig.
Immunohistochemistry did not show specific cellular APO A-II staining in pediatric brain tumor (see supplementary information IV in the online Data Supplement) or healthy cerebellum tissue sections.
A protein cluster at m/z 17 000 that was highly discriminative between tumor and control patients was identified as APO A-II by purification and subsequent peptide mass fingerprinting and MS/MS.