scholarly journals Plasma High-Molecular-Weight and Low-Molecular-Weight Kininogens: Their Structures and Physiological Functions

1977 ◽  
Author(s):  
S. Iwanaga ◽  
H. Kato ◽  
Y.-N. Han ◽  
N. Hashimoto ◽  
T. Sugo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Coagulation Factor ◽  
Disulfide Bridge ◽  
Light Chains ◽  
Low Molecular Weight ◽  
Plasma Kallikrein ◽  
Amino Acid Residues ◽  
Rich Region ◽  
Bovine Plasma ◽  
Structural Differences

Bovine plasma contains two kininogens. One of them, HMW kininogen, has recently been characterized as a new coagulation factor, which is required for the activation of Hageman factor-mediated pathway. To elucidate the structural differences between HMW and LMW kininogens, these were fragmented with plasma kallikrein and snake venom kininogenase, and the resulting products were chemically identified. The kallikrein simultaneously released bradykinin and fragment 1·2 from HMW kininogen. Fragment 1·2 was a histidine-rich glycopeptide consisting of 110 amino acid residues, and its whole sequence and the location of the sugar moieties were established. The venom kininogenase liberated only bradykinin from LMW kininogen. Kinin (and fragment 1·2)-free proteins consisted of heavy and light chains. These chains constituted, respectively, the NH2-and COOH-terminal portions of both parent molecules and were held by a single disulfide bridge. The detailed studies on these chains indicated that the NH2-terminal portions of HMW and LMW kininogens are very similar for each other, whereas their COOH-terminal portions differ significantly. Concerning the results that HMW kininogen overcomes impaired coagulation and fibrinolysis of the kininogen deficient plasmas, and the kinin-free HMW protein has a weak corrective activity, it seems that the histidine-rich region found only in HMW kininogen may be closely related to the functions of the kininogen.

scholarly journals Relationship between structure and correcting activity of bovine high molecular weight kininogen upon the clotting time of fitzgerald-trait plasma

1979 ◽  
Vol 149 (4) ◽  
pp. 847-855 ◽  
Author(s):  
AG Scicli ◽  
R Waldmann ◽  
JA Guimaraes ◽  
G Scicli ◽  
OA Carretero ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Heavy Chain ◽  
Light Chain ◽  
Plasma Kallikrein ◽  
High Molecular Weight Kininogen ◽  
Clotting Time ◽  
Active Inhibitor ◽  
Charged Surfaces ◽  
Bovine Plasma

Bovine high molecular weight kininogen (bHMWK) partially corrects the activated plasma thromboplastin time (aPTT) of Fitzgerald trait plasma which is congenitally deficient in HMWK. The relationship between the structure and activity of HMWK was clarified by studying the effects of different fragments of bHMWK on the aPTT of Fitzgerald-trait plasma. The peptides studied were lys-bradykinin-free HMWK, bradykinin-fragment 1-2-free HMWK, heavy chain, fragment 1-2-light chain, and light chain. All fragments were tested in equimolar concentrations. Bradykinin-fragment 1-2-free HMWK, heavy chain, and light chain have little or no correcting activity upon Fitzgerald-trait plasma aPTr. Fragment 1-2 light chain has the same correcting activity as intact bHMWK, while that of lys-bradykinin-free HMWK appears to be higher. Both fragment 1-2 and fragment 2 inhibit the clotting time of normal human plasma. When compared on a molar basis, fragment 2 is a more active inhibitor than fragment 1-2. When the effects of bovine plasma kallikrein upon bHMWK and hHMWK were studied, it was found that it released kinins from both kininogens. However, while the correcting activity of bHMWK was completely destroyed after 60 min of incubation, that of hHMWK was fully retained. These data suggest that: (a) the active part of bHMWK is comprised of the fragment 1-2 light chain portion; (b) fragment 1-2 or fragment 2 is the binding site to negatively charged surfaces, while the light chain interacts with other components of the surface-mediated reactions; and (c) bovine plasma kallikrein releases kinins, but probably does not cause the release of fragment 1-2 from human HMWK.

Variations in apparent mass of mammalian fast-type myosin light chains correlate with species body size, from shrew to elephant

2007 ◽  
Vol 292 (1) ◽  
pp. R527-R534 ◽  
Author(s):  
Sabahattin Bicer ◽  
Peter J. Reiser
Keyword(s):  
Molecular Weight ◽  
Body Mass ◽  
Mammalian Species ◽  
Actin Binding ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Low Molecular Weight ◽  
Myofibrillar Proteins ◽  
Strongly Correlated ◽  
Electrophoretic Mobilities

A recent study (Bicer S and Reiser PJ. J Muscle Res Cell Motil 25: 623–633, 2004) suggested considerable variation in the apparent molecular mass (Ma), deduced from electrophoretic mobility, in fast-type myosin light chains (MLCF), especially MLC1F, among mammalian species. Furthermore, there was an indication that MLC1F Ma generally correlates with species body mass, over an ∼4,000-fold range in body mass. The results also suggested that Ma of other low-molecular-weight myofibrillar proteins is less variable and not as strongly correlated with body mass among the same species. The objective of this study was to test the hypotheses that the Ma of MLCs does, in fact, vary and correlate with species body mass. The electrophoretic mobilities of MLCF isoforms from 19 species, varying in size ∼500,000-fold, were quantitated. The results confirm that the Ma of MLC1F and MLC2F vary significantly among mammals, spanning a very broad range in body mass; the MLC1F Ma varies more than that of other low-molecular-weight myofibrillar proteins; and there is a significant correlation between species body mass and MLC1F Ma. Differences in MLC1F Ma among five species can be accounted for by differences in the reported amino acid sequence, especially the length of a common polyalanine region near the NH2-terminal actin-binding site. The possibility that the differences in MLC1F sequence among mammalian species, in and adjacent to the actin-binding region, are related to differences in modulation of cross-bridge kinetics in species with diverse locomotion kinetics is discussed.

scholarly journals Studies of the limited degradation of mucus glycoproteins. The effect of dilute hydrogen peroxide

1983 ◽  
Vol 211 (2) ◽  
pp. 323-332 ◽  
Author(s):  
J M Creeth ◽  
B Cooper ◽  
A S R Donald ◽  
J R Clamp
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Simple Structure ◽  
Peptide Bond ◽  
Low Molecular Weight ◽  
Amino Acid Residues ◽  
Oligosaccharide Moiety ◽  
Small Gain ◽  
Mucus Glycoproteins

1. The action of dilute H2O2 on a series of ovarian-cyst glycoproteins and glycopolypeptides was investigated. 2. Both native glycoproteins and the glycopolypeptides were carbohydrate-rich, of relatively low molecular weight and of simple structure. 3. At pH 5.6 and 37 degrees C, exposure to H2O2 for a limited time brought about a partial degradation, the molecular weight being decreased by 2-4-fold. 4. Carbohydrate analysis showed very little change in the oligosaccharide moiety, apart from a small decrease in sialic acid in some samples. 5. Amino acid analysis showed minor changes in serine, threonine and proline contents, but almost total loss of histidine. Concomitantly, there was a small gain in aspartic acid. 6. Myosin, examined at both pH 5.7 and 6.7, exhibited generally similar behaviour, there being losses of other amino acid residues as well as histidine: the viscosity was decreased to a low value, and a range of peptides of widely varying size was produced. 7. It is suggested that attack on the histidine residue, with partial conversion into aspartic acid, is accompanied by scission of the histidyl peptide bond.

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