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The SERS spectra of serums from the healthy persons and rash patients were measured. In the serum of rash, the band of amide I appeared at 1648 cm(-1), while this peak vanished in healthy serums. The relative intensity of 637 cm(-1) assigned to the gauche conformation of C S increased 23% and the band at 725 cm(-1) corresponding to anti-conformation decreases 60%. These indicate that the structure of the protein has changed in serums from the rash patients. The relative intensity at 1449 cm(-1) assigned to the lipids increased nearly one time. The band at 1099 cm(-1) assigned to the Man-D vanished, indicating that the contents of lipids, glucide and protein increased in rash patients. These results may offer a powerful experiment basis for rash diagnosis and biochemistry mechanism study. The multivariae ura statistical methods of principal component analysis (PCA) were also used to analyze the SERS of the serums from healthy persons and rash patients, it can be seen that the regional distribution of rash is wider than healthy volunteers, showing that these serums can be discriminated by PCA.

The SERS spectra were measured from normal and the diabetic serum. In the diabetic serum, the band of amide II shifted to 1 585 cm(-1) and the relative intensity increased 14%, while the relative intensity of 593 cm(-1) which belongs to amide VI reduced 33%. For the protein side chain, the band at 1 368 cm(-1) assigned to the "buried" tryptophan shifted to 1 365 cm(-1) of the "exposed" and the relative intensity reduced 59%. The relative intensity of 635 cm(-1) assigned to the gauche conformation of the C-S decrased 15% and the band at 725 cm(-1) increased 58%. These indicate that the structure of the protein changed in the diabetic serum. The relative intensity at 1 449 cm(-1) assigned to the lipids characteristic increased 58%. The relative intensity of the glucide characteristic at 1 331, 1 099 and 740 cm(-1) increased 35%, 100% and 62%, respectively. So it is indicated that the content of lipids, glucide and protein increased in diabetic. These results may offer a powerful experimental basis for diabetes diagnosis and biochemistry mechanism study.

The quenching reaction of hemoporphyrin with human serum albumin (HSA) was studied by using fluorescence spectraand absorption spectra. The formation constants of them were analyzed at different temperature according to Stem-Volmer equation and double-reciprocal equation, which are smaller at high temperature than at low temperature. The binding site was calculated (r = 4.36) by Foster energy transfer mechanism, and the thermodynamic parameters were obtained. H-bond and Van der Waals are two main reactions between HP and HSA.

Raman spectra of normal and cancer cell from breast cancer patients a represented. It is reported that all of the Ramanlines become weak. The intensities of Raman lines 782 and 1 084 cm(-1) of DNA phosphate group and 1 155 and 1 262 cm(-1) of deoxyribosephosphate decrease. The spectral lines 812 cm(-1) of A-type DNA and 979 and 668 cm(-1) disappear, and the 905 cm(-1) peak is shifted to lower frequency by 6 cm(-1). This means that the phosphate backbone of DNA is destroyed to a certain extent and the fissiparity of cancer cell can't be controlled effectively. In addition, the authors found a kind of Raman line 960 cm(-1) concerning calcificationand sclerosis of cancer cell. The results indicate that Raman spectra may offer the experiment basis for the cancer diagnosis and treatment.

Raman spectra of collagen I at different temperature were obtained. There was no change at 1003 cm(-1) line, 1302 cm(-1) line moved to a higher wave number, but other lines moved to lower wave number when temperature increased. In addition, the authors observed the temperature dependence of Raman intensity and four denaturation points at 0, 40, 68 and 90 degrees C respectively. The points at 40 and 68 degrees C are in agreement with the experimental data by DSC and SHG. The point at 0 degrees C might be frozen transition; the point at 90 degrees C might be related to the damage of secondary structure. When heated to 150 degrees C, the Raman intensity of all bands decreased rapidly and many lines disappeared.

In this paper, the authors obtained Raman spectra of DNA in fiber and aqueous solution at different temperatures. These spectra revealed that the vibration of bases and phosphate group were influenced by varying temperature. Adenine was the most sensitive to varying temperature in all of the vibrational modes. The wave numbers of most of the vibrational modes decreased as the temperature increased except for the band at 1101 cm(-1), and the shift of wave numbers mainly concentrated upon the beginning point of denaturation at 70 degrees C. The temperature dependence of Raman intensity was discussed, and two peaks were obtained at 38 and 82 degrees C, respectively. The results obtained by Raman spectra were in agreement with experimental data by DSC at 82 degrees C. The peak at 38 degrees C was related to the biological activity region of DNA function.

Resonance Raman spectra of single red-cell from human blood are presented by different laser sources. It is reported that there is 1002 cm(-1) line of insensitive conformation of phenylalanine aromatic ring stretching and 1620 cm(-1) line of C-N breathing stretching band of pyrrole ring, which cause strong and sharp resonance lines when excited by 782 nm laser source. They are weaker and the intensity of other lines of high wave number is large and clear when excited by 514 nm laser source. But the intensity of lines of low wave number is strong and clear when excited by 782 nm laser source. At the same time, the authors got Raman spectra lines at different times after taking blood under the same laser source. When using 782 nm laser source, there is no difference except for 1601 cm(-1). There are a lot of weakened lines and lines shifting about 4-10 cm(-1) toward low wave number. The results indicate that Raman spectra may offer the experimental basis for studying structure, function and variability of single red-cell.