In this paper, we use a brand new dataset to estimate and compare wages for casually and annually hired workers in early modern southern Sweden. We ask whether men in either situation could have supported families on the basis of their earnings. Findings indicate that casual earners would have been able to out-earn annual employees for most of the period 1500–1850, but by the eighteenth century wh

The solubility and the emulsification properties of a crude freeze dried alkaline protein extract (APE), 30% protein, obtained from coconut milk press cake by one step extraction at pH 11, were characterized at pH 2 to 11, and the cream and subnatant fractions of the emulsion studied by SDS-PAGE electrophoresis. The protein solubility followed U profile, showing a minimum at pH 3 to 4, close to bu

Freeze-dried coconut press cake powder (CPP), 43% w/w protein, was used to investigate the heat-induced gelation by heating in rheometer to 75℃ in a wide range of pH values, from 4 to 9. Low strain oscillatory method applied the measure visco-elastic propertieson 15% w/w CPP. The gel strength was also assessed by a texture analyzer. SDS-PAGE electrophoresis was conducted to identify the proteins e

Kininogens, the precursor proteins of the vasoactive kinins, bind specifically, reversibly, and saturably to platelets, neutrophils, and endothelial cells. Two domains of the kininogens expose major cell binding sites: domain D3 that is shared by H- and L-kininogen and domain D5H that is exclusively present in H-kininogen. Previously we have mapped the kininogen cell binding sites to 27 residues o

Prekallikrein, the precursor to the serine proteinase kailikrein, circulates in plasma in an equimolar complex with H-kininogen. The binding to H-kininogen is mediated by the kallikrein heavy chain consisting of four "apple" domains, A1-A4, which attaches to H-kininogen with high specificity and affinity (KD = 83 UM). At least two distinct portions of the kallikrein heavy chain form this H-kininog

Prekallikrein, a glycoprotein involved in contact phase activation, circulates in plasma in the form of a binary complex with high molecular weight kininogen (H-kininogen). The binding to H-kininogen is mediated by the prekallikrein heavy chain consisting of four repetitive domains, A1-A4. To define more precisely the region(s) involved in kininogen binding, we have employed an affinity cross-link

High and low molecular mass kininogen, two multidomain plasma proteins, bind to endothelial cells, platelets, and neutrophils in the intravascular compartment. The specific cell attachment site on their common heavy chain is mediated by domain-3, a cystatin-like structure with inhibitory capacity for papain-like proteinases (Jiang, Y., Muller-Esterl, W., and Schmaier, A. H. (1992) J. Biol. Chem. 2

Investigations mapped the region(s) on the light chain of high molecular weight kininogen (HK) that participates in cell binding. Sequential and overlapping peptides of domain 5 (D5(H)) were synthesized to determine its cell binding site(s). Three peptides from non-overlapping regions on D5(H) were found to inhibit biotin-HK binding to endothelial cells. Peptides GKE19 and HNL21 weakly inhibited b

Fever, hypotension and bleeding disorders are common symptoms of sepsis and septic shock. The activation of the contact-phase system is thought to contribute to the development of these severe disease states by triggering proinflammatory and procoagulatory cascades; however, the underlying molecular mechanisms are obscure. Here we report that the components of the contact-phase system are assemble

Activation of polymorphonuclear leukocytes (PMNs) and adhesion to the endothelial lining is a major cause of edema formation. Although known to be dependent on the function of β2 integrins (CD11/CD18), the precise mechanisms by which adherent PMNs may impair endothelial barrier capacity remain unclear. Here, the role of transmembrane signaling by β2 integrins in PMN-induced alterations in tight ju

Human high molecular mass kininogen (HK) participates as nonenzymatic cofactor in the contact system. Here, we show that recombinant domain D5 of HK (rD5) prolongs the clotting time of the intrinsic pathway of coagulation and attenuates the generation of bradykinin. Further studies indicate that a correct fold of domain D5 within HK is required for the activation of the contact system. The folding

Staphylococcus aureus is a prominent human pathogen. Here we report that intact S. aureus bacteria activate the contact system in human plasma in vitro, resulting in a massive release of the potent proinflammatory and vasoactive peptide bradykinin. In contrast, no such effect was recorded with Streptococcus pneumoniae. In the activation of the contact system, blood coagulation factor XII and plasm