Sex, but not skin tone affects penetration of red-light (660 nm) through sites susceptible to sports injury in lean live and cadaveric tissues.

Red-light treatment is emerging as a novel therapy for promoting tissue recovery but data on red-light penetration through human tissues are lacking. We aimed to: (1) determine the effect of light irradiance, tissue thickness, skin tone, sex and bone/muscle content on 660 nm light penetration through common sites of sports injuries, and (2) establish if cadaver tissues serve as a useful model for predicting red-light penetration in live tissues. Live and cadaver human tissues were exposed to 660 nm light at locations across the skull, spinal cord and upper and lower limbs.

Comparison of a salivary 14 kD protein displaying cysteine proteinase inhibitory activity with other salivary cystatins.

An acidic protein with a molecular weight of 14 kD and a cysteine proteinase inhibitory activity was isolated from human whole salive. It was classified therefore as a cystatin. Fractionation of whole saliva by FPLC ion-exchange chromatography, followed by immunochemical analysis with monoclonal antibodies, indicated that this protein, designated 14 kD/E8B, eluted in a single peak, which comprised 6% of the total salivary cystatin-activity.

Characterization of monoclonal antibodies to human salivary (glyco) proteins. Cellular localization of mucin, cystatin-like 14 kD protein and 20 kD glycoprotein in the human submandibular gland.

Using the hybridoma technique, monoclonal antibodies (Mabs) have been produced against three different types of human salivary proteins: high molecular weight mucin, a 20 kD glycoprotein and a 14 kD protein, identified as a member of the cystatin family. The Mabs appeared to be highly specific to their antigen in Elisa and immunoblotting tests. The Mabs were of the IgG-1 (against 20 kD glycoprotein) and IgM (against 14 kD protein and mucin) type.

Isolation and characterization of three non-mucinous human salivary proteins with affinity for hydroxyapatite.

The isolation and chemical analysis of three human salivary proteins is reported. Using cation-exchange, FPLC anion-exchange chromatography and gel filtration, three human salivary proteins with affinity for hydroxyapatite were isolated, having molecular weights of 60 kD, 20 kD and 14 kD, respectively. The 60 kD protein was identified as albumin, and the 14 kD protein as a member of the cystatin family.