Syntheses and Crystal Structures of Two Heterobimetallic Polymeric Cluster Complexes [WS4Ag.cntdot.NH3C(CH2OH)3.cntdot.2DMF]n (Single Chain) and [WS4Ag.cntdot.NH3C(CH2OH)3.cntdot.H2O]n (Double Chain)

1995 ◽  
Vol 34 (20) ◽  
pp. 4931-4932 ◽  
Author(s):  
Qun Huang ◽  
Xintao Wu ◽  
Tianulu Sheng ◽  
Quanming Wang
Keyword(s):  
Crystal Structures ◽  
Single Chain ◽  
Double Chain ◽  
Cluster Complexes ◽  
Polymeric Cluster

scholarly journals Luminescent Ir(iii)–Ln(iii) coordination polymers showing slow magnetization relaxation

2020 ◽  
Vol 7 (23) ◽  
pp. 4580-4592 ◽  
Author(s):  
Kun Fan ◽  
Song-Song Bao ◽  
Ran Huo ◽  
Xin-Da Huang ◽  
Yu-Jie Liu ◽  
...  
Keyword(s):  
Coordination Polymers ◽  
Single Chain ◽  
Double Chain ◽  
Magnetization Relaxation ◽  
Structural Types ◽  
Nir Luminescence

Two structural types of iridium(iii)–lanthanide(iii) coordination polymers, single-chain Ir2Ln and double-chain Ir4Ln2 (Ln = Gd, Dy, Er, and Yb), have been prepared. SMM behaviour and NIR luminescence were observed for the Ir–Er and Ir–Yb systems.

Syntheses and crystal structures of three polymeric cluster compounds +AgMoS4·α-MePyH+n, +AgMoS4·γ-MePyH+n and +AgWS4·γ-MePyH+n

Polyhedron ◽  
1993 ◽  
Vol 12 (7) ◽  
pp. 801-806 ◽  
Author(s):  
Lang Jianping ◽  
Li Jiguo ◽  
Bao Shian ◽  
Xin Xinquan ◽  
Yu Kaibei
Keyword(s):  
Crystal Structures ◽  
Cluster Compounds ◽  
Polymeric Cluster

VESICLE TO MICELLE TRANSITION DRIVEN BY SURFACE SOLID-FLUID TRANSITION

2002 ◽  
Vol 16 (01n02) ◽  
pp. 375-382 ◽  
Author(s):  
JANAKY NARAYANAN ◽  
E. MENDES ◽  
C. MANOHAR
Keyword(s):  
Small Angle ◽  
Fluorescence Anisotropy ◽  
Small Angle Neutron Scattering ◽  
Unique Feature ◽  
Ion Pair ◽  
Single Chain ◽  
Double Chain ◽  
Micellar Phase ◽  
Curvature Energy ◽  
Oppositely Charged

This paper reviews the solution behavior of cetyltrimethylammonium hydroxynaphthalene carboxylate (CTAHNC), which has the unique feature of undergoing a transition from vesicle to worm-like micellar phase in three different ways, namely, increase in temperature, addition of a surfactant and on shearing. Fluorescence anisotropy, NMR, rheology, small angle neutron scattering studies etc gave evidence of the vesicle-micelle transition. CTAHNC can be looked upon as a complex formed by two oppositely charged surfactants (CTA+ and HNC-). This ion pair effectively acts as a double-chain lipid and has a tendency to form vesicles. On increasing the temperature, and/or adding single chain surfactants of shearing, the complex dissociates which changes the curvature energy of the surface. This leads to a 'surface melting' that brings forth the vesicle-micelle transition.

scholarly journals Human tumour cathepsin B. Comparison with normal liver cathepsin B

1992 ◽  
Vol 285 (2) ◽  
pp. 427-434 ◽  
Author(s):  
K Moin ◽  
N A Day ◽  
M Sameni ◽  
S Hasnain ◽  
T Hirama ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Human Liver ◽  
Normal Liver ◽  
Polyacrylamide Gels ◽  
Single Chain ◽  
Human Tumour ◽  
Double Chain ◽  
Normal Human Liver ◽  
Human Cathepsin ◽  
Chain Form

Cathepsin B was purified from normal human liver and several human tumour tissues and partially characterized. Three forms of cathepsin B, with molecular masses of 25 kDa, 26 kDa (the two appearing as a doublet) and 30 kDa, were detected in SDS/polyacrylamide gels. The 25-26 kDa doublet was associated with the fractions from tumours and normal liver containing the highest cathepsin B activity. Cathepsin B from both sources showed similar pH optima. Both normal liver and tumour cathepsin B exhibited similar kinetics against selected synthetic substrates. At neutral pH and 24 degrees C, cathepsin B from both normal liver and tumour exhibited a lower Km and a higher kcat./Km than at pH 6.0. Their inhibitory profiles against synthetic inhibitors were also similar. Immunological studies with a monospecific antibody against the mature double-chain form of human liver cathepsin B and an antibody against a cathepsin B-derived synthetic peptide established the immunological similarity of liver and tumour enzymes. The N-terminal sequences of the 25 kDa and 26 kDa forms were identical with that of the heavy chain of the mature double-chain form of human cathepsin B, whereas the N-terminal sequence of the 30 kDa species was identical with that of the single-chain form of human cathepsin B. Treatment of the double-chain form of cathepsin B from normal liver and tumours with the endoglycosidase peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase converted the 26 kDa form into 25 kDa in SDS/polyacrylamide gels, suggesting that cathepsin B may exist as both glycosylated and unglycosylated forms. Our results, in contrast with those reported earlier for mouse cathepsin B, indicate that human liver and tumour cathepsin B are similar.

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