Nutrition Test 1: Chapter 6

Front 1

amino acids

Back 1

building blocks protein, 22 diff groups, DNA -> RNA
H
cooh-C-Nh2
R

Front 2

R group

Back 2

->s unique characteristics:
hydrophobic, philic, neutral

Front 3

vegetarians

Back 3

be smart!

beans=incomplete protein

no B-12 - only animals - how cells replicate-eventually die

lactovo (best)
vegan - beans

Front 4

complete protein

Back 4

grains + beans
soy = closest to complete

Front 5

nonessential amino acids

Back 5

body already makes

Front 6

essential amino acids

Back 6

9
animal prods = all 9

can't use another to make proteins
right amt, alphabet vowel

Front 7

calculate amt protein need

Back 7

weight/2.2 * .8

Front 8

amino acids linked by...

Back 8

peptide bonds
dipeptide = 2 peptide bonds
need enzymes to break apart peptide bonds

Front 9

amind acid sequence varies w/ diff proteins

Back 9

shape ->s task,

Front 10

hemoglobin

Back 10

globular protein red blood cells, carries O from lungs to cells throughout body

Front 11

protein denaturation

Back 11

uncoil and lose shape ->lose ability
can be irrevers

Front 12

muscle cells

Back 12

can't add them, only make them bigger
eat enough CARBS

Front 13

stomach

Back 13

hydrochloric acid -> hydrolysis of proteins, uncoils, activates stomach enzymes

protein-pepsin, HCL-> smaller polypeptides

Front 14

pancrease and small intenstine

Back 14

pancreative and SI enzymes proteases divide polypeps further -> tri/dipeps, amino acids

*also*
enzymes on surface of SI hydrolyze these peptides to absorb blood carriers in member

Front 15

what amino acids are absorbed?

Back 15

peptides, intestinal and tripeptades, dipeptidases

Front 16

absorption: small intestine

Back 16

proteins decrease amino acids, once amino acids in side SI -> E before absorp

Front 17

misconception with enzymes

Back 17

don't eat enzyme B, predigested proteins (a.a. supplements) NOT easier on body!

Front 18

in the stomach: hydrochloric acid

Back 18

-denatures protein structure
-acctivates pepsinogen to pepsin

Front 19

in the stomach: pepsin

Back 19

- cleaves proteins to smaller polypeps and some free a.a.'s
- stops pesinogen creation

Front 20

in the small intestine: enteropeptidase

Back 20

- changes pancreatic trypsinogen to trypsin

Front 21

in the small intestine: trypsin

Back 21

- stops trysinogen creation
- cleaves peptide bonds next to a.a.'s lysin and arginine
- changes pancreatic procarbxypeptidases to carboxypeptidases
- changes pancreative chymotrypsinogen to chymotrypsin

Front 22

in the small intestine: chymotrypsin

Back 22

- cleaves peptide bonds next to a.a's penylalanine, tyrosinem, tryptophan, methioninem asparagine, and histidine

Front 23

in the small intestine: carboxypeptidases

Back 23

- cleave a.a. from carboxyl ends of polypeptides

Front 24

in the small intestine: elastase and collagenase

Back 24

- cleave poplypes into smaller polypeps and tripeps

Front 25

in the small intestine: intestinal tripeptidases

Back 25

cleave tripeptides to dipeptides and a.a.'s

Front 26

in the small intestien: intestinal dipeptidases

Back 26

glues dipeps to amino acids

Front 27

in the small intestine: intestinal aminopeptidases

Back 27

- attaches amino acid amino ends of small poly peps

Front 28

roles of proteins

Back 28

- enzymes
-building materials for growth/maintenance
-regulators fluid balance
- buffers
- transporters
- source of E and glucose

Front 29

antibodies

Back 29

- defend v disease
- antibodies defend v. antigens -> immunity

Front 30

nitrogen equilibrium

Back 30

N in = N out
- when done w/ growth spurt

Front 31

positive N balance

Back 31

preggers/growing
N in > N out

Front 32

negative N balance

Back 32

-starving
-eating incomplete proteins
-using protein for cals
N in < N out
injury/sick

Front 33

RDA

Back 33

.8 g/kg

weight/2.2 * .8`

Front 34

protein turnover

Back 34

proteins continualy made/broken down

Front 35

amino acid pool

Back 35

supply of a.a.'s (from food protein or body protein) that collects in cells, circulates blood ready to be used

Front 36

deanimating proteins

Back 36

1. striped o N
2. N to urea
3. kidneys filter urea out
4. amino N in pee
5. rest C frags - diff metab pathways

Front 37

using a.a.s to -> proteins/nonessential a.a.'s

Back 37

cells make a.a's they need, make it from another a.a. if not the one they need

Front 38

using a.a.'s to make other compounds

Back 38

ex: neurotransmitters

Front 39

using a.a's to make E and glucose

Back 39

E and glucose
- when no glucose/fatty acids

Front 40

using a.a.'s to make fat

Back 40

when E intake and protein > E needs ---weight gain!

Front 41

protein quality

Back 41

1. digestibility
2. amino acid composition - essential a.a.'s -> proteins and limited amino acid
3. ability to support growth

Front 42

high quality protein

Back 42

have all essential a.a.'s

Front 43

complementary proteins

Back 43

combo dietary proteins make up for lack
ex vegetarians

Front 44

protein digestitbility corrected amino acid score

Back 44

PDCAAS
measure of protein quality
req's for kids and adjusts

Front 45

what is PEM

Back 45

defic of protien, E or both

Front 46

types PEM

Back 46

acute and chronic

Front 47

acute PEM

Back 47

-thin for height
-recent starvation
- leads to Kwashiorkor

Front 48

chronic PEM

Back 48

-short for age
-long term hunger
-small kids easy to overlook b/c look normal

Front 49

Kwashiorkor

Back 49

- acute PEM
- edema
-swollen belly
- protein defic or disease precips
-18 mos -2 yrs old
- 2nd child comes along --> first kid no more breast milk and gets cereal sub